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Gene Review:

SPINK2 - serine peptidase inhibitor, Kazal type 2...

Homo sapiens

Synonyms: Acrosin-trypsin inhibitor, Epididymis tissue protein Li 172, HUSI-II, Serine protease inhibitor Kazal-type 2

Fink, E. et al., Möritz, A. et al., Möritz, A. et al., Dietl, T. et al., Schiessler, H. et al., et al.

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High impact information on SPINK2

The striking similarity in the amino acid sequences which was found previously in HUSI-II and glycoprotein hormone beta-subunits, is neither reflected in codon usage nor in the exon-intron arrangement of the genes [1].
The analysis of this sequence showed that HUSI-II contains a G + C-rich region upstream from the transcription start point (tsp) which fulfills the criteria for a CpG island [1].
A complete cDNA clone encoding the human acrosin-trypsin inhibitor HUSI-II has been isolated from a cDNA library of human testis and completely sequenced [2].
Northern blotting analysis revealed that HUSI-II is synthesized in testis, epididymis and seminal vesicle, but not in the prostate gland [2].
In addition, the HUSI-II sequence shows a striking similarity to the middle part of glycoprotein hormone beta-subunits thus revealing a hitherto unknown structural and evolutionary relationship between Kazal-type inhibitors and glycoprotein hormones [3].

Biological context of SPINK2

The deduced amino acid sequence comprised the complete amino acid sequence of HUSI-II and a putative signal peptide [2].

Anatomical context of SPINK2

The amino acid sequence of the acrosin-trypsin inhibitor HUSI-II from human seminal plasma is presented which unequivocally identifies HUSI-II as being of Kazal-type [3].
Sequence analysis of monkey acrosin-trypsin inhibitor transcripts and their abundant expression in the epididymis [4].
Ejaculated spermatozoa were treated with monospecific antibodies raised in rabbits against HUSI-I and HUSI-II, respectively, and with fluorescein-labeled IgG from goat directed against the rabbit IgG [5].

Regulatory relationships of SPINK2

Variants of human seminal acrosin inhibitor (HUSI-II) which inhibit human leukocyte elastase [6].

Other interactions of SPINK2

Amino acid sequence elucidation of human acrosin-trypsin inhibitor (HUSI-II) reveals that Kazal-type proteinase inhibitors are structurally related to beta-subunits of glycoprotein hormones [3].
The inhibitor from human seminal plasma HUSI-II may therefore be seen as the natural antagonist of the sperm protease acrosin [7].

Analytical, diagnostic and therapeutic context of SPINK2

Molecular cloning and sequence analysis of the cDNA encoding the human acrosin-trypsin inhibitor (HUSI-II) [2].

References

Organization and sequence of the gene encoding the human acrosin-trypsin inhibitor (HUSI-II). Möritz, A., Grzeschik, K.H., Wingender, E., Fink, E. Gene (1993) [Pubmed]
Molecular cloning and sequence analysis of the cDNA encoding the human acrosin-trypsin inhibitor (HUSI-II). Möritz, A., Lilja, H., Fink, E. FEBS Lett. (1991) [Pubmed]
Amino acid sequence elucidation of human acrosin-trypsin inhibitor (HUSI-II) reveals that Kazal-type proteinase inhibitors are structurally related to beta-subunits of glycoprotein hormones. Fink, E., Hehlein-Fink, C., Eulitz, M. FEBS Lett. (1990) [Pubmed]
Sequence analysis of monkey acrosin-trypsin inhibitor transcripts and their abundant expression in the epididymis. Perry, A.C., Jones, R., Hall, L. Biochim. Biophys. Acta (1993) [Pubmed]
Localization of seminal plasma proteinase inhibitors in human spermatozoa as revealed by the indirect immunofluorescence technique. Dietl, T., Kruck, J., Schill, W.B., Fritz, H. Hoppe-Seyler's Z. Physiol. Chem. (1976) [Pubmed]
Variants of human seminal acrosin inhibitor (HUSI-II) which inhibit human leukocyte elastase. Collins, J., Taube, W., Fink, E., Möritz, A., Fritz, H. Biomed. Biochim. Acta (1991) [Pubmed]
Inhibitors of acrosin and granulocyte proteinases from human genital tract secretions. Schiessler, H., Arnhold, M., Ohlsson, K., Fritz, H. Hoppe-Seyler's Z. Physiol. Chem. (1976) [Pubmed]

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