New insights into the origin, structure and role of CD52: a major component of the mammalian sperm glycocalyx.

TY - JOUR

T1 - New insights into the origin, structure and role of CD52: a major component of the mammalian sperm glycocalyx.

AU - Kirchhoff, C

AU - Schröter, S

N1 - Copyright 2001 S. Karger AG, Basel

PY - 2001

Y1 - 2001

N2 - The sperm glycocalyx represents the primary interface between the male gamete and its environment, and gamete interaction inevitably involves interaction with this structure. Thus, it has potential significance as a target for antibodies that inhibit sperm function. Still, little is known about the components and biological role of the sperm glycocalyx. Despite the apparent complexity of the sperm membrane, surface carbohydrate labelling experiments show a high selectivity suggesting that carbohydrate side chains of CD52, an unusually short, bipolar glycopeptide of epididymal origin, form major components of the sperm glycocalyx in all mammalian species investigated. Acquisition of the highly sialylated, lipid-anchored CD52 antigen is one of the few well-defined modifications that occur to the sperm membrane during epididymal passage. It would explain changes in lectin-binding patterns and also the remarkable surface charge differences occurring during epididymal transit, most probably attributable to its terminal sialic acid residues. CD52 seems to be immunodominant on human spermatozoa, and antibodies directed against it can agglutinate and completely immobilize human sperm in the presence of complement. Expression of the same peptide backbone in lymphocytes had largely discounted its consideration as a candidate for contraceptive development. However, the recent proof of male-specific modifications indicates the feasibility of this approach.

AB - The sperm glycocalyx represents the primary interface between the male gamete and its environment, and gamete interaction inevitably involves interaction with this structure. Thus, it has potential significance as a target for antibodies that inhibit sperm function. Still, little is known about the components and biological role of the sperm glycocalyx. Despite the apparent complexity of the sperm membrane, surface carbohydrate labelling experiments show a high selectivity suggesting that carbohydrate side chains of CD52, an unusually short, bipolar glycopeptide of epididymal origin, form major components of the sperm glycocalyx in all mammalian species investigated. Acquisition of the highly sialylated, lipid-anchored CD52 antigen is one of the few well-defined modifications that occur to the sperm membrane during epididymal passage. It would explain changes in lectin-binding patterns and also the remarkable surface charge differences occurring during epididymal transit, most probably attributable to its terminal sialic acid residues. CD52 seems to be immunodominant on human spermatozoa, and antibodies directed against it can agglutinate and completely immobilize human sperm in the presence of complement. Expression of the same peptide backbone in lymphocytes had largely discounted its consideration as a candidate for contraceptive development. However, the recent proof of male-specific modifications indicates the feasibility of this approach.

KW - Animals

KW - Antigens, CD

KW - Antigens, Neoplasm

KW - Carbohydrate Sequence

KW - Glycocalyx

KW - Glycoproteins

KW - Humans

KW - Male

KW - Mammals

KW - Molecular Sequence Data

KW - Sequence Homology, Amino Acid

KW - Spermatozoa

U2 - 10.1159/000016810

DO - 10.1159/000016810

M3 - SCORING: Journal article

C2 - 11114591

VL - 168

SP - 93

EP - 104

JO - CELLS TISSUES ORGANS

JF - CELLS TISSUES ORGANS

SN - 1422-6405

IS - 1-2

M1 - 1-2

ER -