Research

The structural mechanism of trypsin-induced intrinsic motility in Manduca sexta spermatozoa in vitro


Reference:

Friedlander, M., Jeshtadi, A. and Reynolds, S. E., 2001. The structural mechanism of trypsin-induced intrinsic motility in Manduca sexta spermatozoa in vitro. Journal of Insect Physiology, 47 (3), pp. 245-255.

Related documents:

This repository does not currently have the full-text of this item.
You may be able to access a copy if URLs are provided below.

Abstract

Lepidopteran males produce eupyrene (nucleate) and apyrene (anucleate) spermatozoa, bur in the female only eupyrene spermatozoa leave the spermatheca and fertilize the eggs. Both kinds of spermatozoa lack intrinsic motility in the male genital duct. They become motile in the spermatophore. in a process involving proteases from the male duct. In vitro, trypsin induces immotile spermatozoa to become motile. We studied the changes spermatozoa of Manduca sexta undergo during trypsin-induced motility and found that (a) they mimick rather closely those occurring in vivo during normal sperm maturation in genital ducts and (b) they are time- and dose-dependent. As in vivo. they comprise, successively. (a) disappearance of an extracellular matrix that maintains the integrity of eupyrene bundles in the seminal vesicle. (b) dispersion of the eupyrene bundles and intermingling of eupyrene and apyrene spermatozoa and ic) "hatching" of eupyrene spermatozoa from individual enclosing envelopes that are formed in the seminal vesicle. "Hatching" may not directly be related to motility since eupyrene spermatozoa become motile before "hatching" and motile apyrene spermatozoa never "hatch". Rather "hatching" may be related to the capacitation of eupyrene spermatozoa to either leave the spermatheca or fertilize the eggs. or both, as neither apyrene spermatozoa, nor those eupyrene spermatozoa that fail to "hatch". leave the spermatheca. (C) 2001 Elsevier Science Ltd. All rights reserved.

Details

Item Type Articles
CreatorsFriedlander, M., Jeshtadi, A. and Reynolds, S. E.
DepartmentsFaculty of Science > Biology & Biochemistry
RefereedYes
StatusPublished
ID Code4360
Additional InformationID number: ISI:000167073200004

Export

Actions (login required)

View Item