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Plasma sex steroid binding in Chiroptera.

G G Kwiecinski, D A Damassa, A W Gustafson

Biology of Reproduction

|April 1, 1987

Summary

Researchers identified a specific sex steroid-binding protein (SBP) in some bat species, which binds androgens and estradiol, similar to primates. Corticosteroid-binding globulin (CBG) was also found in most bats, binding glucocorticoids and androgens.

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Area of Science:

Comparative endocrinology
Mammalian reproductive biology
Biochemistry of steroid transport

Background:

Steroid-binding proteins play crucial roles in hormone transport and bioavailability.
Understanding these proteins across diverse mammalian species provides insights into evolutionary adaptations.
Bats, with their unique physiology, offer a valuable model for studying steroid hormone regulation.

Purpose of the Study:

To investigate the presence and characteristics of plasma steroid-binding proteins in various bat species.
To compare steroid-binding protein profiles across different bat families and relate them to primate patterns.
To determine the binding affinities of identified proteins for key steroid hormones.

Main Methods:

Plasma samples from seven bat species across four families were analyzed.
Steady-state polyacrylamide gel electrophoresis was employed to identify specific binding proteins.
Binding affinities for androgens (testosterone, dihydrotestosterone) and estradiol were assessed.

Main Results:

A specific sex steroid-binding protein (SBP) was identified in phyllostomid and vespertilionid bats.
This bat SBP demonstrated high affinity for androgens and estradiol, mirroring primate SBP.
A specific SBP was absent in the vampire bat and pteropodids; corticosteroid-binding globulin (CBG) was present in most species, binding glucocorticoids and androgens.

Conclusions:

Sex steroid-binding protein (SBP) with primate-like binding characteristics exists in certain bat lineages.
Corticosteroid-binding globulin (CBG) in bats exhibits broader binding, including androgens, beyond its known glucocorticoid function.
These findings highlight conserved and divergent evolutionary pathways of steroid-binding proteins in mammals.

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