Premium
Formyl‐met—leu—phe induces chemotaxis and acrosomal enzyme release in bull sperm
Author(s) -
Vijayasarathy S.,
Shivaji S.,
Iqbal M.,
Balaram P.
Publication year - 1980
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(80)81162-8
Subject(s) - unit (ring theory) , library science , chemistry , polymer science , mathematics , computer science , mathematics education
The chemical nature of the factors that induce the selective fusion and vesiculation of the outer acrosomal and plasma membranes in sperm cells is yet to be established [1,2]. This process, known as the acrosome reaction, precedes fertilisation of the egg and is accompanied by the release of the degradative enzymes sequestered in the acrosomal vesicle of sperm [l]. The synthetic tripeptide, formyl-Met-Leu-Phe has been shown to induce chemotaxis in rabbit neutrophils [3]. It also causes the release of lysosomal enzymes, a process which must necessarily involve a fusion of the lysosomal and plasma membranes [4]. Functional analogies between lysosomes and the acrosome in sperm have been drawn [5,6]. Here we describe the selective release of bull sperm acrosomal enzymes, induced by formyl-Met-leu-Phe. The specificity of this process is established by the inability of related di- and tripeptide analogs to cause enzyme release. Further, formyl-Met-Leu-Phe is also shown to induce chemotaxis in bull sperm. This observation demonstrates for the first time that low molecular weight peptides may indeed be capable of stimulating release of acrosomal contents, a process closely identified with the acrosome reaction.