RXFP1 Is Expressed on the Sperm Acrosome, and Relaxin Stimulates the Acrosomal Reaction of Human Spermatozoa

Glycocalyx is the name given by Bennett to the extracellular glycoprotein coat present in some cell surfaces. It appears to play an important role in cell properties such as antigenicity, cell adhesivity, specific permeability, and ATP ase activity. In the sperm this coat can be directly related to such important phenomena as capacitation and fertilization. The presence of glycocalyx in invertebrate spermatozoa has already been demonstrated. Recently Yanagimachi et al. has determined the negative charges on sperm surfaces of mammalian spermatozoa including man, using colloidal iron hydroxide. No mention was made however of the outer surface coat as composed of substances other than those confering a negative charge. The purpose of this work was therefore to determine the presence of a glycocalyx in human spermatozoa using alcian blue and lanthanum staining.

Download Full-text

A High Resolution Cytochemical Study of Nuclear ATPase in Human Spermatozoa

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100116590 ◽

1975 ◽

Vol 33 ◽

pp. 594-595

Author(s):

A. Sosa ◽

L. Calzada

Keyword(s):

High Resolution ◽

Atpase Activity ◽

Nuclear Membrane ◽

Human Sperm ◽

Sperm Nucleus ◽

Human Spermatozoa ◽

Cytochemical Study ◽

Membrane Bound ◽

Sperm Nuclei ◽

Interchromatin Space

The dependence of nuclear metabolism on the function of the nuclear membrane is not well understood. Whether or not the function of the nuclear membrane is partial or totally responsible of the repressed template activity of human sperm nucleus has not at present been elucidated. One of the membrane-bound enzymatic activities which is concerned with the mechanisms whereby substances are thought to cross cell membranes is adenosintriphosphatase (ATPase). This prompted its characterization and distribution by high resolution photogrammetry on isolated human sperm nuclei. Isolated human spermatozoa nuclei were obtained as previously described. ATPase activity was demonstrated by the method of Wachstein and Meisel modified by Marchesi and Palade. ATPase activity was identified as dense and irregularly distributed granules confined to the internal leaflet of the nuclear membrane. Within the nucleus the appearance of the reaction product occurs as homogenous and dense precipitates in the interchromatin space.

Download Full-text

The extracellular matrix of echinoderm and amphibian eggs: Visualization in quick-frozen, deep-etched, and rotary-shadowed specimens

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s042482010015784x ◽

1990 ◽

Vol 48 (3) ◽

pp. 60-61

Author(s):

Barry Bonnell ◽

Carolyn Larabell ◽

Douglas Chandler

Keyword(s):

Extracellular Matrix ◽

Plasma Membrane ◽

Sea Urchin ◽

Crystalline Structure ◽

Cortical Granule ◽

Two Dimensional ◽

Small Peptides ◽

Deep Etching ◽

Quick Freezing ◽

Acrosomal Reaction

Eggs of many species including those of echinoderms, amphibians and mammals exhibit an extensive extracellular matrix (ECM) that is important both in the reception of sperm and in providing a block to polyspermy after fertilization.In sea urchin eggs there are two distinctive coats, the vitelline layer which contains glycoprotein sperm receptors and the jelly layer that contains fucose sulfate glycoconjugates which trigger the acrosomal reaction and small peptides which act as chemoattractants for sperm. The vitelline layer (VL), as visualized by quick-freezing, deep-etching, and rotary-shadowing (QFDE-RS), is a fishnet-like structure, anchored to the plasma membrane by short posts. Orbiting above the VL are horizontal filaments which are thought to anchor the thicker jelly layer to the egg. Upon fertilization, the VL elevates and is transformed by cortical granule secretions into the fertilization envelope (FE). The rounded casts of microvilli in the VL are transformed into angular peaks and the envelope becomes coated inside and out with sheets of paracrystalline protein having a quasi-two dimensional crystalline structure.

Download Full-text