Newly identified water-borne protein pheromones interact with attractin to stimulate mate attraction in Aplysia

Scott F. Cummins, Amy E. Nichols, Catherine H. Schein, Gregg Thomas Nagle

Research output: Contribution to journalReview article

31 Citations (Scopus)

Abstract

The water-borne protein attractin is a potent sex pheromone involved in forming and maintaining mating and egg-laying aggregations in the marine mollusk Aplysia. Binary blends of attractin and either enticin, temptin, or seductin, three other Aplysia protein pheromones, stimulate mate attraction. The four pheromones are thought to act in concert during egg-laying. The new data presented here show that: (1) the water-borne odor of non-laying Aplysia brasiliana further increases the attractiveness of attractin and of eggs in T-maze bioassays. This suggests that individual Aplysia release additional factors that enhance the effects of attractin, enticin, temptin, and seductin during egg-laying; (2) the N-terminal region of enticin aligns well with the conserved epidermal growth factor (EGF)-like domain of mammalian reproductive proteins known as fertilins, which may mediate intercellular adhesion interactions between eggs and sperm; (3) temptin, according to fold recognition servers, may also have an EGF-like fold. Enticin and temptin also have conserved metal binding sequences that may play a role in their signaling behavior. These results suggest that aspects of mammalian egg-sperm interactions (fertilins) may have evolved from pheromonal signaling mechanisms. We also review the structure, expression, localization, release, and behavioral actions of attractin, enticin, temptin, and seductin.

Original languageEnglish (US)
Pages (from-to)597-606
Number of pages10
JournalPeptides
Volume27
Issue number3
DOIs
StatePublished - Mar 1 2006

Fingerprint

Aplysia
Pheromones
Sperm-Ovum Interactions
Ovum
Epidermal Growth Factor
Water
Sex Attractants
Proteins
Bioassay
Odors
Mollusca
Servers
Adhesion
Agglomeration
Metals
Biological Assay
Eggs
Fertilins

Keywords

  • Aplysia
  • Attractin
  • Enticin
  • Fertilin
  • Fibrillin
  • Pheromone
  • Seductin
  • Temptin

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Endocrinology
  • Cellular and Molecular Neuroscience

Cite this

Newly identified water-borne protein pheromones interact with attractin to stimulate mate attraction in Aplysia. / Cummins, Scott F.; Nichols, Amy E.; Schein, Catherine H.; Nagle, Gregg Thomas.

In: Peptides, Vol. 27, No. 3, 01.03.2006, p. 597-606.

Research output: Contribution to journalReview article

Cummins, Scott F. ; Nichols, Amy E. ; Schein, Catherine H. ; Nagle, Gregg Thomas. / Newly identified water-borne protein pheromones interact with attractin to stimulate mate attraction in Aplysia. In: Peptides. 2006 ; Vol. 27, No. 3. pp. 597-606.
@article{af8daadb104b4dfc868d9a3b138d4792,
title = "Newly identified water-borne protein pheromones interact with attractin to stimulate mate attraction in Aplysia",
abstract = "The water-borne protein attractin is a potent sex pheromone involved in forming and maintaining mating and egg-laying aggregations in the marine mollusk Aplysia. Binary blends of attractin and either enticin, temptin, or seductin, three other Aplysia protein pheromones, stimulate mate attraction. The four pheromones are thought to act in concert during egg-laying. The new data presented here show that: (1) the water-borne odor of non-laying Aplysia brasiliana further increases the attractiveness of attractin and of eggs in T-maze bioassays. This suggests that individual Aplysia release additional factors that enhance the effects of attractin, enticin, temptin, and seductin during egg-laying; (2) the N-terminal region of enticin aligns well with the conserved epidermal growth factor (EGF)-like domain of mammalian reproductive proteins known as fertilins, which may mediate intercellular adhesion interactions between eggs and sperm; (3) temptin, according to fold recognition servers, may also have an EGF-like fold. Enticin and temptin also have conserved metal binding sequences that may play a role in their signaling behavior. These results suggest that aspects of mammalian egg-sperm interactions (fertilins) may have evolved from pheromonal signaling mechanisms. We also review the structure, expression, localization, release, and behavioral actions of attractin, enticin, temptin, and seductin.",
keywords = "Aplysia, Attractin, Enticin, Fertilin, Fibrillin, Pheromone, Seductin, Temptin",
author = "Cummins, {Scott F.} and Nichols, {Amy E.} and Schein, {Catherine H.} and Nagle, {Gregg Thomas}",
year = "2006",
month = "3",
day = "1",
doi = "10.1016/j.peptides.2005.08.026",
language = "English (US)",
volume = "27",
pages = "597--606",
journal = "Peptides",
issn = "0196-9781",
publisher = "Elsevier Inc.",
number = "3",

}

TY - JOUR

T1 - Newly identified water-borne protein pheromones interact with attractin to stimulate mate attraction in Aplysia

AU - Cummins, Scott F.

AU - Nichols, Amy E.

AU - Schein, Catherine H.

AU - Nagle, Gregg Thomas

PY - 2006/3/1

Y1 - 2006/3/1

N2 - The water-borne protein attractin is a potent sex pheromone involved in forming and maintaining mating and egg-laying aggregations in the marine mollusk Aplysia. Binary blends of attractin and either enticin, temptin, or seductin, three other Aplysia protein pheromones, stimulate mate attraction. The four pheromones are thought to act in concert during egg-laying. The new data presented here show that: (1) the water-borne odor of non-laying Aplysia brasiliana further increases the attractiveness of attractin and of eggs in T-maze bioassays. This suggests that individual Aplysia release additional factors that enhance the effects of attractin, enticin, temptin, and seductin during egg-laying; (2) the N-terminal region of enticin aligns well with the conserved epidermal growth factor (EGF)-like domain of mammalian reproductive proteins known as fertilins, which may mediate intercellular adhesion interactions between eggs and sperm; (3) temptin, according to fold recognition servers, may also have an EGF-like fold. Enticin and temptin also have conserved metal binding sequences that may play a role in their signaling behavior. These results suggest that aspects of mammalian egg-sperm interactions (fertilins) may have evolved from pheromonal signaling mechanisms. We also review the structure, expression, localization, release, and behavioral actions of attractin, enticin, temptin, and seductin.

AB - The water-borne protein attractin is a potent sex pheromone involved in forming and maintaining mating and egg-laying aggregations in the marine mollusk Aplysia. Binary blends of attractin and either enticin, temptin, or seductin, three other Aplysia protein pheromones, stimulate mate attraction. The four pheromones are thought to act in concert during egg-laying. The new data presented here show that: (1) the water-borne odor of non-laying Aplysia brasiliana further increases the attractiveness of attractin and of eggs in T-maze bioassays. This suggests that individual Aplysia release additional factors that enhance the effects of attractin, enticin, temptin, and seductin during egg-laying; (2) the N-terminal region of enticin aligns well with the conserved epidermal growth factor (EGF)-like domain of mammalian reproductive proteins known as fertilins, which may mediate intercellular adhesion interactions between eggs and sperm; (3) temptin, according to fold recognition servers, may also have an EGF-like fold. Enticin and temptin also have conserved metal binding sequences that may play a role in their signaling behavior. These results suggest that aspects of mammalian egg-sperm interactions (fertilins) may have evolved from pheromonal signaling mechanisms. We also review the structure, expression, localization, release, and behavioral actions of attractin, enticin, temptin, and seductin.

KW - Aplysia

KW - Attractin

KW - Enticin

KW - Fertilin

KW - Fibrillin

KW - Pheromone

KW - Seductin

KW - Temptin

UR - http://www.scopus.com/inward/record.url?scp=33644667225&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=33644667225&partnerID=8YFLogxK

U2 - 10.1016/j.peptides.2005.08.026

DO - 10.1016/j.peptides.2005.08.026

M3 - Review article

C2 - 16309784

AN - SCOPUS:33644667225

VL - 27

SP - 597

EP - 606

JO - Peptides

JF - Peptides

SN - 0196-9781

IS - 3

ER -