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Karyorrhexis
Karyorrhexis
Karyorrhexis
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Apoptosis

Karyorrhexis (from Greek κάρυον karyon, "kernel, seed, nucleus," and ῥῆξις rhexis, "bursting") is the destructive fragmentation of the cell nucleus that occurs in a dying cell.[1] It is characterized by the breakdown of the nuclear envelope and the dispersal of condensed chromatin into the cytoplasm.[2] The process is usually preceded by pyknosis (irreversible chromatin condensation) and followed by karyolysis (enzymatic dissolution of chromatin). It may occur during programmed cell death (apoptosis), cellular senescence, or necrosis. [citation needed]

In apoptosis, karyorrhexis is mediated by Ca2+- and Mg2+-dependent endonucleases, ensuring that nuclear fragments are packaged into apoptotic bodies and removed by phagocytosis. In necrosis, by contrast, nuclear fragmentation occurs in a less orderly fashion, leaving behind cellular debris that can contribute to tissue damage and inflammation.[3]

  • Morphological features of pyknosis and other forms of nuclear destruction
    Morphological features of pyknosis and other forms of nuclear destruction
  • Microscopy of an apoptotic neutrophil with nuclear fragmentation (H&E stain)
    Microscopy of an apoptotic neutrophil with nuclear fragmentation (H&E stain)

Nuclear envelope dissolution

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In the intrinsic pathway of apoptosis, cellular stressors such as oxidative stress activate pro-apoptotic members of the Bcl-2 protein family, leading to permeabilization of the mitochondrial outer membrane.[4] This releases cytochrome c into the cytoplasm, triggering a signaling cascade that culminates in the activation of multiple caspase enzymes.[4] Among these, caspase-6 cleaves nuclear lamina proteins such as lamin A/C, structural components that maintain the integrity of the nuclear envelope. Their cleavage facilitates the controlled dissolution of the nuclear envelope during apoptosis.[5]

Chromatin fragmentation

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During karyorrhexis in apoptosis, nuclear DNA is cleaved in an orderly fashion by endonucleases such as caspase-activated DNase, producing discrete nucleosomal fragments.[6] This organization is possible because DNA has already undergone condensation during pyknosis, being tightly wrapped around histone proteins in repeating units of ≈180 bp. Activated endonucleases cleave the linker DNA between histones, generating short, regularly sized fragments that correspond to nucleosomal units.[7] These DNA fragments can be visualized by gel electrophoresis, where they produce a characteristic “ladder” pattern, a hallmark used to distinguish apoptosis from other forms of cell death.[8]

In other forms of cell death

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In apoptosis, karyorrhexis is a controlled process in which caspases degrade lamin proteins, leading to the orderly breakdown of the nuclear envelope. In less regulated forms of cell death, such as necrosis, nuclear degradation occurs through different mechanisms. Necrotic cells are characterized by rupture of the plasma membrane, lack of caspase activation, and the induction of an inflammatory response.[3] Because necrosis is caspase-independent, the nucleus may remain intact during early stages before rupturing as a result of osmotic stress and membrane damage.

A specialized form of necrosis, necroptosis, involves a more regulated pathway but still results in plasma membrane rupture. Here, nuclear destabilization is mediated by the protease calpain, which cleaves lamins and promotes nuclear envelope breakdown.[3]

Unlike karyorrhexis in apoptosis, which generates apoptotic bodies subsequently removed by phagocytosis, karyorrhexis in necroptosis leads to the uncontrolled release of intracellular contents into the extracellular space, where they are cleared primarily through pinocytosis.[9]

Mechanism

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Apoptotic pathways

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Apoptosis, and the associated nuclear degradation through karyorrhexis, can be triggered by a variety of physiological and pathological stimuli. DNA damage, oxidative stress, hypoxia, and infections activate signaling cascades that converge on the intrinsic apoptotic pathway. This pathway may also be induced by external factors such as ethanol, which promotes activation of apoptosis-related proteins including BAX and caspases.[10]

In addition to intrinsic signals, activation of cell-surface death receptors such as CD95 can initiate the extrinsic apoptotic pathway, also resulting in caspase activation and nuclear envelope degradation.[5] In both pathways, executioner caspases, particularly caspase-3, cleave nuclear lamins and promote chromatin fragmentation, driving karyorrhexis.[3]

Necrotic pathways

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In contrast to apoptosis, nuclear degradation during necrosis is a largely unregulated process. Necrotic cells are characterized by rupture of the plasma membrane, uncontrolled calcium influx, and activation of proteases such as calpain, which accelerate nuclear disintegration.[11] These features highlight the mechanistic differences between necrotic and apoptotic karyorrhexis.

Senescence and DNA damage response

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The extent of DNA damage can also determine whether a cell undergoes apoptosis or enters cellular senescence. Senescence involves a permanent cessation of cell division and is typically observed after approximately 50 doublings in primary cells.[12]

One major cause of senescence is telomere shortening, which triggers a persistent DNA damage response (DDR). This response activates the kinases ATR and ATM, which in turn activate Chk1 and Chk2. These signaling events stabilize the transcription factor p53. When DNA damage is mild, p53 induces CIP proteins that inhibit CDKs, enforcing cell-cycle arrest. In cases of severe DNA damage, however, p53 activates apoptotic pathways, leading to caspase activity and nuclear envelope dissolution via karyorrhexis.[13]

Clinical significance

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Karyorrhexis is a hallmark of cell death observed in a range of pathological conditions, including ischemia and neurodegenerative disorders. It has been documented in myocardial infarction and stroke, where nuclear fragmentation contributes to tissue damage during acute stress responses.[14] In obstetric pathology, placental vascular malperfusion has been linked to karyorrhexis and implicated in cases of fetal demise, reflecting its role in disrupted tissue homeostasis.[15]

In oncology, apoptotic karyorrhexis has a dual significance. On one hand, it contributes to controlled cell death and tumor suppression; on the other, resistance to apoptosis allows cancer cells to evade this process, promoting malignancy. Therapeutic strategies that target apoptotic pathways aim to restore nuclear degradation and trigger tumor regression.[16]

See also

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References

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Revisions and contributorsEdit on WikipediaRead on Wikipedia

Karyorrhexis

View on Grokipedia
from Grokipedia
Karyorrhexis is the fragmentation of the cell nucleus into small, irregular pieces, characterized by the contraction and clumping of chromatin followed by the loss of the nuclear boundary, serving as a key morphological indicator of cell death in pathological processes such as necrosis and apoptosis. In the context of necrosis, an uncontrolled form of cell death triggered by severe injury or noxious stimuli, karyorrhexis represents one of the three classic nuclear alterations, typically following pyknosis (nuclear shrinkage and chromatin condensation) and preceding karyolysis (nuclear dissolution). This fragmentation occurs as part of the broader necrotic process, which involves cellular swelling, rupture of organelles and the plasma membrane, and subsequent inflammation due to the release of intracellular contents. Karyorrhexis is readily observable under light microscopy with hematoxylin and eosin staining, appearing as nuclear "dust" or pyknotic debris, and it underscores the irreversible damage in affected tissues. Although most prominently associated with , karyorrhexis also features in , a programmed and energy-dependent mechanism, where it manifests as the breakdown of the nucleus into discrete fragments prior to the formation of apoptotic bodies. In apoptotic cells, this nuclear change accompanies cytoplasmic shrinkage and membrane blebbing, contrasting with the swelling seen in . The presence of karyorrhexis in histological samples aids pathologists in distinguishing these pathways and diagnosing underlying conditions, such as ischemic injury, infections, or malignancies. In specific clinical applications, like the risk stratification of neuroblastic tumors, the mitosis-karyorrhexis index quantifies the number of cells undergoing or karyorrhexis to predict and guide treatment.

Fundamentals

Definition and Etymology

Karyorrhexis is the destructive fragmentation of the that occurs during , characterized by the breakdown of the and the dispersal of condensed into the as irregularly distributed basophilic nuclear fragments. The term derives from the Greek words karyon, meaning "nucleus" or "kernel," and rhexis, meaning "bursting" or "rupture," reflecting the process of nuclear disintegration. As a hallmark of irreversible cell death, karyorrhexis is typically observed under light microscopy as shrunken, fragmented nuclei that stain intensely with hematoxylin, distinguishing it from viable cells. It follows pyknosis and precedes karyolysis in the sequence of nuclear changes during necrosis.

Role in Cell Death Pathways

Karyorrhexis occupies a central position as an intermediate stage in the nuclear alterations characteristic of classical necrosis, occurring after pyknosis—in which chromatin undergoes irreversible clumping and condensation—and before karyolysis, the final complete dissolution and fading of nuclear chromatin. This sequence reflects the progression from early reversible injury to irreversible cell demise in unregulated necrotic pathways, where cellular swelling and membrane rupture lead to inflammatory responses. In apoptotic , karyorrhexis manifests as a highly regulated nuclear fragmentation, integral to the controlled disassembly of the cell without eliciting , in stark contrast to the passive, damage-induced process in . Here, it follows condensation and contributes to the formation of apoptotic bodies containing nuclear fragments, ensuring orderly clearance by . Similarly, in necroptosis—a programmed necrotic pathway—karyorrhexis appears as a morphological hallmark akin to classical , signaling commitment to lytic , while in senescence-associated processes, it serves as an indicator of terminal progression toward death in irreparably damaged cells. The process of karyorrhexis exhibits evolutionary conservation across eukaryotic organisms, underscoring its fundamental role in cascades as a mechanism to sequester and eliminate damaged genetic material, thereby preventing its propagation and maintaining genomic integrity at the organismal level.

Morphological Features

Nuclear Envelope Dissolution

Karyorrhexis begins with the progressive loss of nuclear membrane integrity, which compromises the barrier between the nucleus and , resulting in the blurring of nuclear boundaries observable under . This initial breakdown disrupts the structural continuity of the , allowing for the subsequent disintegration of nuclear architecture. The process marks a critical early event in nuclear fragmentation during , distinguishing it from reversible cellular stresses. Visualization of nuclear envelope dissolution in karyorrhexis relies on established microscopy techniques that reveal these morphological alterations. microscopy highlights fragmented remnants of the nuclear envelope, including dilated pore spaces and invaginations, providing high-resolution evidence of structural disassembly. In contrast, light microscopy of histological sections shows indistinct nuclear margins and loss of clear boundary definition, often appearing as hazy or irregular outlines around the condensing . These imaging approaches confirm the envelope's breakdown as a hallmark of karyorrhexis, preceding the dispersal of nuclear material.

Chromatin Condensation and Fragmentation

In karyorrhexis, undergoes a progressive transformation beginning with hypercondensation following , where the aggregates into a dense, shrunken mass within the nucleus. This stage is marked by intense due to the compaction of , reflecting irreversible cellular damage in necrotic processes. Subsequently, the hypercondensed fragments into discrete, basophilic chunks that disperse irregularly throughout the , appearing as small pyknotic masses under light microscopy. These fragments stain darkly with basic dyes such as hematoxylin, highlighting their dense composition and aiding histological identification of karyorrhectic cells. The dispersal is facilitated by concurrent dissolution, which permits the pieces to scatter without containment. Biochemically, this fragmentation results from non-specific DNA cleavage into irregular pieces, producing a heterogeneous smear pattern on rather than the uniform nucleosomal units seen in apoptotic DNA degradation. Such irregular breaks disrupt the overall nuclear architecture, contributing to the complete loss of nuclear integrity and the cell's terminal disintegration in .

Molecular Mechanisms

Apoptotic Pathways

Karyorrhexis in is initiated through two primary regulated pathways: the intrinsic mitochondrial pathway, triggered by cellular stresses such as DNA damage or , and the extrinsic death receptor pathway, activated by extracellular signals from ligands binding to death receptors like Fas or TNF receptors. Both pathways converge on the activation of initiator (such as in the extrinsic route or caspase-9 in the intrinsic route), which subsequently trigger a caspase cascade involving effector like caspase-3 and caspase-6. This enzymatic amplification ensures the orderly dismantling of nuclear components, culminating in karyorrhexis as a hallmark of . A critical step in nuclear envelope breakdown during karyorrhexis is the cleavage of lamin A/C by caspase-6, which disrupts the and facilitates fragmentation of the nucleus into discrete pieces. Studies in caspase-6-deficient models demonstrate that this cleavage is essential for proper nuclear disassembly, as uncleaved lamin A/C inhibits the progression to karyorrhexis. Concurrently, caspase-3 activates DNase caspase-activated DNase (CAD) by cleaving its inhibitor ICAD, allowing CAD to enter the nucleus and fragment into nucleosomal units of approximately 180 base pairs. This internucleosomal cleavage produces the characteristic DNA "ladder" pattern observable on , distinguishing apoptotic karyorrhexis from other modes. Additional chromatin cleavage is mediated by calcium- and magnesium-dependent endonucleases, which further degrade DNA into smaller fragments following CAD activity. These enzymes contribute to the complete nuclear fragmentation while the process remains controlled, preventing release of intracellular contents. The resulting nuclear fragments are packaged into membrane-bound apoptotic bodies, which are rapidly phagocytosed by neighboring cells or macrophages, ensuring a non-inflammatory resolution of cell death.

Necrotic and Necroptotic Pathways

In classical , karyorrhexis arises from uncontrolled cellular injury leading to plasma membrane rupture and massive influx of extracellular calcium ions into the . This calcium overload activates calcium-dependent proteases known as calpains, which proteolytically cleave proteins such as , compromising the integrity of the and facilitating nuclear fragmentation. Concurrently, the elevated calcium levels promote the activity of endonucleases like DNase I, resulting in irregular, non-specific cleavage of genomic DNA and contributing to the disorganized nuclear breakdown characteristic of karyorrhexis. In necroptosis, a form of regulated necrosis, karyorrhexis is triggered through the receptor-interacting protein kinase (RIPK) pathway involving RIPK1, RIPK3, and mixed lineage kinase domain-like (MLKL) proteins. Upon activation, RIPK3 phosphorylates MLKL, inducing its oligomerization and translocation to the plasma membrane, where it disrupts membrane integrity and causes permeabilization, allowing ion influx including calcium. This secondary calcium elevation activates calpains, which mediate nuclear envelope degradation and chromatin fragmentation, while the process also promotes the release of inflammatory cytokines such as IL-1β through NLRP3 inflammasome activation. Unlike the uniform DNA processing in apoptotic pathways, this leads to chaotic nuclear dispersal.00058-7.pdf) The DNA fragments generated during both necrotic and necroptotic karyorrhexis are heterogeneous in size, ranging from high molecular weight smears to random breaks without a defined pattern, dispersing into the and exacerbating secondary via damage-associated molecular pattern (DAMP) release. This irregular fragmentation contrasts with more structured processes in other modes and underscores the pro-inflammatory nature of these pathways.

Senescence-Associated Processes

is often triggered by progressive shortening, which limits to approximately 50 divisions in human fibroblasts, known as the . This attrition generates DNA damage signals that activate the /p21 pathway, leading to arrest and the formation of persistent DNA damage foci marked by γ-H2AX. These foci represent sites of uncapped s recognized as double-strand breaks, sustaining a chronic DNA damage response without progressing to full . In senescent cells, nuclear architecture undergoes reorganization, including the formation of senescence-associated foci (SAHF), which are compact, macroH2A-enriched domains that repress proliferation-associated genes. SAHF assembly contributes to partial instability, as increased nuclear fragility promotes blebbing and localized disruptions without complete dissolution. This results in chromatin fragmentation, manifesting as DNA breaks and micronuclei, yet cells remain viable and do not undergo full . Such changes overlap briefly with apoptotic DNA damage triggers but persist in a non-lethal state. This incomplete karyorrhexis-like process, characterized by ongoing nuclear blebbing and unresolved DNA breaks, sustains the (SASP), where proinflammatory factors are secreted to influence the tissue microenvironment. Persistent nuclear alterations in senescent cells thus drive tissue dysfunction and aging by promoting chronic inflammation and impairing regenerative capacity.

Distinctions from Pyknosis and Karyolysis

Karyorrhexis represents a distinct mid-stage nuclear alteration in the progression of , characterized by the active fragmentation of the previously condensed chromatin mass into discrete, irregularly shaped nuclear fragments that are visible under light as shrunken, basophilic particles scattered throughout the . This process follows , the initial irreversible condensation and clumping of into a dense, homogeneous, basophilic mass, which shrinks the nucleus and increases its density, often appearing as a small, dark-staining structure. Unlike , which primarily involves compaction without breakdown, karyorrhexis involves enzymatic and mechanical disruption leading to irreversible nuclear disintegration. In contrast, karyolysis occurs as the terminal stage, involving the complete enzymatic dissolution of the nuclear through digestion by endonucleases such as DNase γ, resulting in a pale, faded nucleus that loses its affinity for nuclear stains like hematoxylin, eventually appearing as an empty or ghost-like structure. This differs markedly from karyorrhexis, where distinct, fragmented nuclear pieces remain identifiable for a period, allowing for clear microscopic differentiation before full dissolution. thus signifies advanced autolysis or heterolysis, with the chromatin being progressively degraded into soluble , unlike the particulate remnants in karyorrhexis. Within the necrotic sequence, these changes unfold in a temporal progression observable via : emerges early, typically within 12-24 hours post- as seen in models like , marking the onset of irreversible damage; follows as the intermediate phase, becoming prominent between 1-3 days with visible fragmentation; and dominates in the late stage, extending to several days where nuclear outlines blur and dissolve entirely. This timeline varies by tissue type, injury severity, and environmental factors but generally spans hours to days, aiding pathologists in estimating injury duration.

Nuclear Changes in Other Cell Death Modes

In autophagy, a process often associated with cellular self-digestion rather than overt , the nucleus is typically spared from significant morphological alterations, with the formation of perinuclear vacuoles and autophagosomes occurring without fragmentation or nuclear breakdown. Karyorrhexis, characterized by the nuclear fragmentation prominent in necrotic , is absent in pure autophagic responses unless the process progresses to secondary , where nuclear disintegration may ensue as a terminal event. Ferroptosis, an iron-dependent form of regulated driven by , exhibits minimal nuclear involvement, preserving nuclear integrity without condensation, margination, or fragmentation that defines karyorrhexis. This contrasts sharply with the prominent nuclear and subsequent karyorrhexis observed in , as ferroptotic cells prioritize cytoplasmic and mitochondrial damage over nuclear changes. In , an inflammasome-mediated lytic , gasdermin family proteins form plasma membrane pores that lead to cellular swelling and rupture, but the nucleus generally remains intact without the fragmentation typical of . Instead, late-stage pyroptotic events may include nuclear rounding or random DNA fragmentation, though these do not progress to the disseminated nuclear pieces seen in ; hybrid features, such as partial , can emerge in mixed death modes involving pyroptosis and necroptosis.

Clinical and Pathological Relevance

Associations with Diseases

Karyorrhexis, as a hallmark of nuclear fragmentation in necrotic and apoptotic cell death, is prominently observed in ischemic conditions such as myocardial infarction, where it appears in the histology of affected cardiac tissue around 3 to 4 days post-infarction, coinciding with neutrophil infiltration and early phagocytosis by macrophages. In stroke pathology, particularly in ischemic infarcts, karyorrhexis contributes to the nuclear breakdown in neuronal necrosis, often following pyknosis in the evolving infarct core, serving as an indicator of irreversible tissue damage in both adult and perinatal cases. Hypoxia-induced necrosis, a common sequela of ischemia, frequently exhibits karyorrhexis in vulnerable brain regions like the hippocampus and basal ganglia, with histological studies showing its prevalence in perinatal hypoxic-ischemic injuries where fragmented nuclei correlate with the extent of neuronal loss. In neurodegenerative diseases, karyorrhexis is linked to nuclear fragmentation driven by apoptotic pathways, as seen in where cleaved caspase-3 activation leads to karyorrhexis alongside tau-related pathology, contributing to neuronal loss in affected regions. Similarly, in , evidence of in the from animal models includes karyorrhexis, reflecting degeneration and supporting its role as a of progressive cellular demise. Beyond ischemia and neurodegeneration, karyorrhexis features in other pathological contexts, such as placental malperfusion leading to fetal demise, where clustered villous stromal-vascular karyorrhexis indicates fetal vascular obstruction and reduced perfusion, often correlating with adverse outcomes like or . In infections causing acute , such as Kikuchi-Fujimoto disease, karyorrhexis accompanies patchy necrotic areas in lymph nodes, highlighting its utility in identifying histiocytic necrotizing processes. Toxin-induced , including from mitochondrial toxin exposures like 3-nitropropionic acid, displays karyorrhexis during the fragmentation phase in affected cells. In cancer, evasion of karyorrhexis-associated enables tumor cell survival and progression, with dysregulated anti-apoptotic pathways allowing neoplastic cells to resist nuclear fragmentation and promote uncontrolled proliferation.

Implications for Diagnosis and Therapy

Karyorrhexis, as a hallmark of nuclear fragmentation in regulated pathways, plays a key role in clinical diagnostics through targeted assays that detect associated molecular changes. Immunohistochemical staining for cleaved , particularly A/C fragmented by caspase-6, serves as a reliable marker for apoptotic karyorrhexis in tissue biopsies, enabling quantification of caspase-dependent in tumors and enabling correlation with prognostic factors. Similarly, the detects DNA strand breaks characteristic of karyorrhexis in apoptotic and necrotic processes, facilitating its use in biopsies for assessing in conditions like kidney injury or disorders, though it requires combination with morphological evaluation to distinguish pathways. In , the mitosis-karyorrhexis index (MKI), which counts mitotic figures and karyorrhectic nuclei per 5,000 tumor cells, provides independent prognostic value in , stratifying risk and guiding therapy intensity, with high MKI (>200/5,000 cells) associated with poorer outcomes independent of age and tumor grade. Recent advances include artificial intelligence-based models for automated morphological classification and prediction of MKI status in , enhancing diagnostic efficiency and prognostic assessment. Therapeutically, promoting karyorrhexis via induction offers a strategy for targeting cancer cells, exemplified by BH3 mimetics like , which inhibit to unleash pro-apoptotic proteins, leading to mitochondrial outer membrane permeabilization and subsequent nuclear fragmentation in tumors such as and . Ongoing research on modulation continues to explore enhancements in apoptotic nuclear disassembly for improved efficacy against resistant cancers, including solid tumors. Conversely, inhibiting necroptotic karyorrhexis mitigates inflammatory damage in ischemic conditions; blockers, such as necrostatin-1, prevent RIPK1-mediated necroptosis, reducing neuronal and myocardial injury post-ischemia-reperfusion by blocking downstream MLKL activation and nuclear breakdown. In senescence-associated aging diseases, senolytics such as and selectively induce in senescent cells, potentially triggering karyorrhexis to clear dysfunctional cells and alleviate pathologies like neurodegeneration, though clinical translation remains investigational.

References

  1. https://www.ncbi.nlm.nih.gov/medgen/137694
  2. https://www.ncbi.nlm.nih.gov/books/NBK557627/
  3. https://pmc.ncbi.nlm.nih.gov/articles/PMC4230251/
  4. https://pmc.ncbi.nlm.nih.gov/articles/PMC6340950/
  5. https://pmc.ncbi.nlm.nih.gov/articles/PMC2117903/
  6. https://pubmed.ncbi.nlm.nih.gov/35570824/
  7. https://www.sciencedirect.com/topics/neuroscience/karyorrhexis
  8. https://www.merriam-webster.com/medical/karyorrhexis
  9. https://vmicro.iusm.iu.edu/hs_vm/docs/glossary.pdf
  10. https://www.ahajournals.org/doi/10.1161/01.STR.26.4.636
  11. https://www.sciencedirect.com/topics/agricultural-and-biological-sciences/karyorrhexis
  12. https://pmc.ncbi.nlm.nih.gov/articles/PMC4785073/
  13. https://www.ncbi.nlm.nih.gov/books/NBK499821/
  14. https://pmc.ncbi.nlm.nih.gov/articles/PMC4480161/
  15. https://www.nature.com/articles/s41418-017-0012-4
  16. https://www.sciencedirect.com/topics/[neuroscience](/page/Neuroscience)/karyorrhexis
  17. https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/karyorrhexis
  18. https://www.nature.com/articles/srep15623
  19. https://pmc.ncbi.nlm.nih.gov/articles/PMC7171462/
  20. https://pmc.ncbi.nlm.nih.gov/articles/PMC3261451/
  21. https://jeccr.biomedcentral.com/articles/10.1186/1756-9966-30-87
  22. https://www.thermofisher.com/us/en/home/life-science/antibodies/antibodies-learning-center/antibodies-resource-library/cell-signaling-pathways/cellular-apoptosis-pathway.html
  23. https://www.ahajournals.org/doi/10.1161/01.RES.82.11.1111
  24. https://pmc.ncbi.nlm.nih.gov/articles/PMC125972/
  25. https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0006234
  26. https://www.sciencedirect.com/topics/neuroscience/caspase-activated-dnase
  27. https://www.nature.com/articles/4401161
  28. https://pmc.ncbi.nlm.nih.gov/articles/PMC8891305/
  29. https://pubmed.ncbi.nlm.nih.gov/10807908/
  30. https://www.nature.com/articles/s41420-020-0256-5
  31. https://pmc.ncbi.nlm.nih.gov/articles/PMC1851179/
  32. https://www.nature.com/articles/4400627
  33. https://pmc.ncbi.nlm.nih.gov/articles/PMC5520172/
  34. https://www.nature.com/articles/s41418-018-0172-x
  35. https://pmc.ncbi.nlm.nih.gov/articles/PMC9308588/
  36. https://pmc.ncbi.nlm.nih.gov/articles/PMC10669395/
  37. https://pmc.ncbi.nlm.nih.gov/articles/PMC2802848/
  38. https://www.sciencedirect.com/science/article/pii/S1097276504002564
  39. https://www.cell.com/fulltext/S1534-5807%2804%2900408-3
  40. https://www.mdpi.com/2073-4409/11/2/273
  41. https://www.jci.org/articles/view/95148
  42. https://pmc.ncbi.nlm.nih.gov/articles/PMC6983664/
  43. https://www.sciencedirect.com/topics/biochemistry-genetics-and-molecular-biology/karyolysis
  44. https://emedicine.medscape.com/article/1960472-overview
  45. https://www.nature.com/articles/cddis2013217
  46. https://www.nature.com/articles/s41419-023-06154-8
  47. https://www.nature.com/articles/s41392-020-00428-9
  48. https://www.nature.com/articles/s41422-020-00441-1
  49. https://www.nature.com/articles/s41392-021-00507-5
  50. https://www.nature.com/articles/s41418-018-0106-7
  51. https://www.nature.com/articles/s41419-023-06382-y
  52. https://webpath.med.utah.edu/CVHTML/CV024.html
  53. https://www.pathologystudent.com/what-happens-after-brain-tissue-dies/
  54. https://pubmed.ncbi.nlm.nih.gov/9292869/
  55. https://pmc.ncbi.nlm.nih.gov/articles/PMC9380082/
  56. https://academic.oup.com/jnen/article/65/9/873/2646727
  57. https://www.pathologyoutlines.com/topic/placentafetaldeath.html
  58. https://pubmed.ncbi.nlm.nih.gov/9777391/
  59. https://pmc.ncbi.nlm.nih.gov/articles/PMC6573656/
  60. https://pmc.ncbi.nlm.nih.gov/articles/PMC3197541/
  61. https://pubmed.ncbi.nlm.nih.gov/16434901/
  62. https://www.sciencedirect.com/science/article/pii/S0304383513005466
  63. https://link.springer.com/article/10.1007/s00418-007-0356-9
  64. https://www.researchgate.net/publication/348202187_TUNEL_Assay_A_Powerful_Tool_for_Kidney_Injury_Evaluation
  65. https://ascopubs.org/doi/10.1200/JCO.19.03285
  66. https://ascopubs.org/doi/10.1200/JCO.2024.42.16_suppl.10023
  67. https://pmc.ncbi.nlm.nih.gov/articles/PMC8775468/
  68. https://www.atsjournals.org/doi/pdf/10.1164/rccm.201510-2106CI
  69. https://www.frontiersin.org/journals/bioengineering-and-biotechnology/articles/10.3389/fbioe.2022.823945/full
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