Definition and research guide
This page combines a MeSH definition, publication statistics and selected research abstracts. It is a starting point for reading the literature, not a medical textbook or a systematic evidence review.
Content available: 4 complete abstracts (682 words), 10 references. Full article text is not stored or reproduced here; follow the PMID, DOI or PMC links to read the original sources and their access terms.
Definition
The anterior portion of the spermatozoon (spermatozoa) that contains mainly the nucleus with highly compact chromatin material.
Definition: NLM Medical Subject Headings (MeSH) scope note (Public domain (U.S. National Library of Medicine); attribution requested). View the MeSH record.
Also known as: Head, Sperm; Heads, Sperm; Sperm Heads.
Where it fits in the MeSH classification
- Broader topics
- Spermatozoa
- Narrower topics
- Acrosome
Related concepts
Research landscape
PubMed indexes 6,058 records tagged with the MeSH heading “Sperm Head” (counts retrieved 2026-10-31). 519 of them (8.6%) were published from 2020 onward, and the busiest period so far is through 1999 with 3,151 records.
Reviews account for 304 records (5.0%) and meta-analyses for 1. Randomized controlled trials number 14 (0.2%) as a share of all records on the topic. Randomized trials make up only a small share of this literature, so much of what is known comes from laboratory, observational or descriptive work.
Show the data
| Period | Records |
|---|---|
| through 1999 | 3,151 |
| 2000-2009 | 1,184 |
| 2010-2019 | 1,204 |
| 2020 onward | 519 |
Publication-type chart data
| Type | Records | Share |
|---|---|---|
| Reviews | 304 | 5.0% |
| Meta-analyses | 1 | 0.0% |
| Randomized controlled trials | 14 | 0.2% |
Method: PubMed query "Sperm Head"[MeSH Terms] with publication-type and date filters, retrieved 2026-10-31.
Reading the evidence in anatomy and physiology
Anatomy describes how body structures are built and physiology describes how they normally work, so most findings here are descriptive or mechanistic rather than evidence about treatment. Much of what is known comes from dissection, imaging, tissue studies and experiments in animals, and measurements in healthy volunteers can differ from those in people with disease or at different ages. Normal ranges vary between individuals and populations. Check whether a result was measured in people or in another species, the age and health of the participants, and the method used.
Evidence from open-access studies
These open-access studies come from PubMed’s best-match results for this heading (papers whose main topic it is), ranked here by citation count, with one recent addition. Each abstract is reproduced in full under its recorded open licence so that you can read the authors’ own words. They illustrate the literature; they are not a systematic summary of it. Citation counts measure attention, not reliability or clinical benefit.
| Study / authors | Year | Source label / design | Europe PMC citations | Licence / source |
|---|---|---|---|---|
| Mammalian sperm head formation involves different polarization of two novel LINC complexes | 2010 | Research article Design not recorded in structured metadata | 128 | cc by PMID 20711465 · DOI · PMC2919408 |
| Essential role for SUN5 in anchoring sperm head to the tail | 2017 | Research article Design not recorded in structured metadata | 108 | cc by PMID 28945193 · DOI · PMC5634783 |
| Globozoospermia and lack of acrosome formation in GM130-deficient mice | 2017 | Research article Design not recorded in structured metadata | 72 | cc by PMID 28055014 · DOI · PMC5386352 |
| Molecular models of the sperm head-tail coupling apparatus | 2025 | Review article Design not recorded in structured metadata | 4 | cc by PMID 41058548 · DOI · PMC12539209 |
Mammalian sperm head formation involves different polarization of two novel LINC complexes [1]
Abstract reading summary — source excerpts
- Opening excerpt
- BackgroundLINC complexes are nuclear envelope bridging protein structures formed by interaction of SUN and KASH proteins.
- Closing excerpt
- Together, our findings suggest that theses LINC complexes connect the differentiating spermatid nucleus to surrounding cytoskeletal structures to enable its well-directed shaping and elongation, which in turn is a critical parameter for male fertility.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (209 words)
BackgroundLINC complexes are nuclear envelope bridging protein structures formed by interaction of SUN and KASH proteins. They physically connect the nucleus with the peripheral cytoskeleton and are critically involved in a variety of dynamic processes, such as nuclear anchorage, movement and positioning and meiotic chromosome dynamics. Moreover, they are shown to be essential for maintaining nuclear shape.FindingsBased on detailed expression analysis and biochemical approaches, we show here that during mouse sperm development, a terminal cell differentiation process characterized by profound morphogenic restructuring, two novel distinctive LINC complexes are established. They consist either of spermiogenesis-specific Sun3 and Nesprin1 or Sun1eta, a novel non-nuclear Sun1 isoform, and Nesprin3. We could find that these two LINC complexes specifically polarize to opposite spermatid poles likely linking to sperm-specific cytoskeletal structures. Although, as shown in co-transfection/immunoprecipitation experiments, SUN proteins appear to arbitrarily interact with various KASH partners, our study demonstrates that they actually are able to confine their binding to form distinct LINC complexes.ConclusionsFormation of the mammalian sperm head involves assembly and different polarization of two novel spermiogenesis-specific LINC complexes. Together, our findings suggest that theses LINC complexes connect the differentiating spermatid nucleus to surrounding cytoskeletal structures to enable its well-directed shaping and elongation, which in turn is a critical parameter for male fertility.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 20711465 · DOI · PMC2919408
Essential role for SUN5 in anchoring sperm head to the tail [2]
Abstract reading summary — source excerpts
- Opening excerpt
- SUN (Sad1 and UNC84 domain containing)-domain proteins are reported to reside on the nuclear membrane playing distinct roles in nuclear dynamics.
- Closing excerpt
- Our studies reveal the essential role of SUN5 in anchoring sperm head to the tail and provide a promising way to treat this kind of acephalic spermatozoa-associated male infertility.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (150 words)
SUN (Sad1 and UNC84 domain containing)-domain proteins are reported to reside on the nuclear membrane playing distinct roles in nuclear dynamics. SUN5 is a new member of the SUN family, with little knowledge regarding its function. Here, we generated Sun5-/- mice and found that male mice were infertile. Most Sun5-null spermatozoa displayed a globozoospermia-like phenotype but they were actually acephalic spermatozoa. Additional studies revealed that SUN5 was located in the neck of the spermatozoa, anchoring sperm head to the tail, and without functional SUN5 the sperm head to tail coupling apparatus was detached from nucleus during spermatid elongation. Finally, we found that healthy heterozygous offspring could be obtained via intracytoplasmic injection of Sun5-mutated sperm heads for both male mice and patients. Our studies reveal the essential role of SUN5 in anchoring sperm head to the tail and provide a promising way to treat this kind of acephalic spermatozoa-associated male infertility.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 28945193 · DOI · PMC5634783
Globozoospermia and lack of acrosome formation in GM130-deficient mice [3]
Abstract reading summary — source excerpts
- Opening excerpt
- Globozoospermia is a common reproductive disorder that causes male infertility in humans, and the malformation or loss of acrosomes is the prominent feature of this disease.
- Closing excerpt
- Thus, the GM130-deficient mouse provides a valuable model for investigating the etiology of human globozoospermia.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (177 words)
Globozoospermia is a common reproductive disorder that causes male infertility in humans, and the malformation or loss of acrosomes is the prominent feature of this disease. Although the acrosome is thought to be derived from the Golgi apparatus, the detailed molecular mechanisms remain unclear. GM130 is a cis-side localized Golgi matrix protein,whereas the physiological functions of this protein remain elusive. Here we showed that inactivation of GM130-caused male infertility in mouse model. The primary defects were the absence of acrosomes, round sperm heads, and aberrant assembly of the mitochondrial sheath, which comprise the characteristic features of human globozoospermia. Further investigation indicated that loss of GM130 did not affect the secretion of pro-acrosomic vesicles, whereas the vesicles failed to fuse into a single large acrosome vesicle. Co-localization of the adaptor protein complex AP1 and trans-Golgi network (TGN) protein TGN46 was disrupted, suggesting that the malformation of acrosomes is most likely due to the defect in the sorting and coating of Golgi-derived pro-acrosomic vesicles. Thus, the GM130-deficient mouse provides a valuable model for investigating the etiology of human globozoospermia.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 28055014 · DOI · PMC5386352
Molecular models of the sperm head-tail coupling apparatus [4]
Abstract reading summary — source excerpts
- Opening excerpt
- A stable connection between the sperm head (nucleus) and tail (flagellum) is crucial for proper fertility.
- Closing excerpt
- Finally, we discuss outstanding questions in the field and how future studies might delineate the complex molecular machinery at the HTCA.
- Interpretation limits
- Verbatim excerpts from the authors’ abstract; the closing excerpt may describe a finding, limitation or recommendation. Design, population, effect size and uncertainty have not been independently extracted or appraised. Read the complete abstract and linked paper before interpreting the findings.
Read complete abstract (146 words)
A stable connection between the sperm head (nucleus) and tail (flagellum) is crucial for proper fertility. This linkage is mediated by centrioles, or their remnants, at a structure known as the head-tail coupling apparatus (HTCA). Although many proteins have been implicated at the HTCA, the precise molecular linkage that connects the head and tail is poorly understood. This Review proposes three molecular models for the HTCA based on the presence of three key components: nuclear envelope proteins, cytoplasmic proteins and centriole proteins. As it relates to these models, we discuss the current literature that describes the linkage from nuclear envelope proteins to cytosolic and centriole proteins, including a LINC-complex-based linkage, a nuclear pore complex linkage and a direct linkage that bypasses the outer nuclear membrane. Finally, we discuss outstanding questions in the field and how future studies might delineate the complex molecular machinery at the HTCA.
Abstract reproduced from the open-access article under the recorded cc by licence; © the authors. PMID 41058548 · DOI · PMC12539209
Key reviews and meta-analyses
The most cited review-type papers among PubMed’s best-match results for this heading, listed with bibliographic details only. Follow the links for the full text and access terms.
- Research article The acrosome-acroplaxome-manchette complex and the shaping of the spermatid head [5]
- Research article Intramanchette transport (IMT): managing the making of the spermatid head, centrosome, and tail [6]
- Research article Mammalian sperm acrosome: formation, contents, and function [7]
- Research article Early events in mammalian fertilization [8]
- Research article Sperm head membrane reorganisation during capacitation [9]
- Research article Molecular events mediating sperm activation [10]
References
- Göb E, Schmitt J, Benavente R, Alsheimer M. Mammalian sperm head formation involves different polarization of two novel LINC complexes. . 2010. PMID 20711465 · DOI · PMC2919408
- Shang Y, Zhu F, Wang L, Ouyang YC, Dong MZ, Liu C, et al.. Essential role for SUN5 in anchoring sperm head to the tail. . 2017. PMID 28945193 · DOI · PMC5634783
- Han F, Liu C, Zhang L, Chen M, Zhou Y, Qin Y, et al.. Globozoospermia and lack of acrosome formation in GM130-deficient mice. . 2017. PMID 28055014 · DOI · PMC5386352
- Buglak DB, Galletta BJ, Rusan NM. Molecular models of the sperm head-tail coupling apparatus. . 2025. PMID 41058548 · DOI · PMC12539209
- Kierszenbaum AL, Tres LL. The acrosome-acroplaxome-manchette complex and the shaping of the spermatid head. Arch Histol Cytol. 2004. PMID 15700535 · DOI
- Kierszenbaum AL. Intramanchette transport (IMT): managing the making of the spermatid head, centrosome, and tail. Mol Reprod Dev. 2002. PMID 12211054 · DOI
- Abou-Haila A, Tulsiani DR. Mammalian sperm acrosome: formation, contents, and function. Arch Biochem Biophys. 2000. PMID 10898932 · DOI
- Wassarman PM. Early events in mammalian fertilization. Annu Rev Cell Biol. 1987. PMID 3318876 · DOI
- Gadella BM, Tsai PS, Boerke A, Brewis IA. Sperm head membrane reorganisation during capacitation. Int J Dev Biol. 2008. PMID 18649260 · DOI
- Ward CR, Kopf GS. Molecular events mediating sperm activation. Dev Biol. 1993. PMID 8392473 · DOI
About this article
- Sources
- NLM Medical Subject Headings (definition, synonyms); NCBI PubMed (counts, identifiers); Europe PMC (open-access abstracts and citation counts).
- Verification
- Every reference was resolved against PubMed on 2026-10-31; title, year and DOI matched.
- Review state
- automated source verified; no human expert review has been recorded yet.
- Version
- 1, last updated 2026-10-31.
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Evidence strength
EvidenceHelix's computed view of the study designs behind this topic: how common meta-analyses, randomized trials and reviews are, how recent the literature is, and a plain-language reading. It describes the design mix of the literature. It is not a quality appraisal of any study, and it is not medical advice.