Document Detail


Functional and immunological analysis of the human sperm proteome.
MedLine Citation:
PMID:  22459723     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
This is a review of ten previously published studies of the human sperm proteome. Proteins expressed on the sperm cell surface were identified and characterized by a combination of vectorial labelling with radioiodine and biotin, PI-PLC treatment, two-dimensional gel electrophoresis, immuno and lectin blotting procedures, affinity overlay assays with radioactive nucleotide triphosphates and 45Ca, and mass spectrometry analysis. Examination of capacitation-induced modifications of the human sperm proteome led to the cloning and characterisation of two new phospho-regulated cancer-testis antigens, which we named Fibrous Sheath Protein 95 (FSP95) and CABYR (calcium-binding tyrosine phosphorylation regulated). A protein kinase A RII binding domain is present between amino acids 124 and 141 identifying FSP95 (now commonly known as AKAP3) as a member of the A kinase anchoring protein-family which provides spatial and temporal specificity to the cAMP-PKA pathway. In addition to scaffolding PKA, PDE and protein phosphatases, AKAPs also bind to a group of four proteins that share homology to the RII dimerization/docking (R2D2) domain of PKA' regulatory subunit. CABYR, which is one of these four proteins, also interacts with a diverse array of signal tranducers via its SH3-, R2D2-, and proline-rich extension-like domains. AKAP3 and CABYR appear to associate in high molecular weight multi-protein complexes, which regulate the flagella' energy supply and movements. Diagonal gel electrophoresis experiments suggest that the high molecular weight signal-integrating scaffold partly is established by homo- and hetero-oligomerization of lower molecular weight splice variants of CABYR. The putative role of CABYR in lung cancer cells is finally discussed.
Authors:
Søren Naaby-Hansen
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Danish medical journal     Volume:  59     ISSN:  2245-1919     ISO Abbreviation:  Dan Med J     Publication Date:  2012 Apr 
Date Detail:
Created Date:  2012-03-30     Completed Date:  2012-08-02     Revised Date:  2012-09-06    
Medline Journal Info:
Nlm Unique ID:  101576205     Medline TA:  Dan Med J     Country:  Denmark    
Other Details:
Languages:  eng     Pagination:  B4414     Citation Subset:  IM    
Affiliation:
Department of Clinical Immunology, Aalborg Sygehus Nord, Aarhus University Hospital, 9000 Aalborg, Denmark. sonh@rn.dk
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MeSH Terms
Descriptor/Qualifier:
Antibodies / immunology
Autoimmunity / genetics,  immunology
Databases, Factual
Electrophoresis, Gel, Pulsed-Field
Glycosylphosphatidylinositols / immunology
Humans
Male
Proteome / genetics,  immunology*
Spermatogenesis / genetics
Spermatozoa / immunology*
Chemical
Reg. No./Substance:
0/Antibodies; 0/Glycosylphosphatidylinositols; 0/Proteome

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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