TY - JOUR
T1 - Phylogenetic Survey of Proteins Related to Synapsin I and Biochemical Analysis of Four Such Proteins from Fish Brain
AU - Goelz, Susan E.
AU - Nestler, Eric J.
AU - Greengard, Paul
PY - 1985/7
Y1 - 1985/7
N2 - Abstract: A phylogenetic survey of proteins immunologically related to Synapsin I, a major synaptic vesicle‐associated phosphoprotein in mammals was carried out. Proteins antigenically related to Synapsin I were found by use of radioimmunoassay and other radioimmunochemical techniques in the nervous systems of several vertebrate and invertebrate species, which included birds, reptiles, amphibians, fish, echinoderms, arthropods, and mollusks. Four proteins present in fish brain, antigenically related to Synapsin I, were further studied and found to resemble mammalian Synapsin I in several respects. Like Synapsin I, the fish proteins were present in high amounts in nervous tissue, were enriched in synaptosomal fractions of brain where they were substrates for endogenous protein kinases, were acid extractable, and were sensitive to digestion by collagenase. In addition, two‐dimensional peptide‐mapping analysis revealed some homology between major phosphopeptide fragments of Synapsin I and the fish proteins. The results indicate that proteins related to Synapsin I are widespread in the animal kingdom.
AB - Abstract: A phylogenetic survey of proteins immunologically related to Synapsin I, a major synaptic vesicle‐associated phosphoprotein in mammals was carried out. Proteins antigenically related to Synapsin I were found by use of radioimmunoassay and other radioimmunochemical techniques in the nervous systems of several vertebrate and invertebrate species, which included birds, reptiles, amphibians, fish, echinoderms, arthropods, and mollusks. Four proteins present in fish brain, antigenically related to Synapsin I, were further studied and found to resemble mammalian Synapsin I in several respects. Like Synapsin I, the fish proteins were present in high amounts in nervous tissue, were enriched in synaptosomal fractions of brain where they were substrates for endogenous protein kinases, were acid extractable, and were sensitive to digestion by collagenase. In addition, two‐dimensional peptide‐mapping analysis revealed some homology between major phosphopeptide fragments of Synapsin I and the fish proteins. The results indicate that proteins related to Synapsin I are widespread in the animal kingdom.
KW - Fish
KW - Phosphopro‐teins
KW - Phylogenetic survey
KW - Protein I
KW - Synapsin I
UR - http://www.scopus.com/inward/record.url?scp=0021810190&partnerID=8YFLogxK
U2 - 10.1111/j.1471-4159.1985.tb05475.x
DO - 10.1111/j.1471-4159.1985.tb05475.x
M3 - Article
C2 - 2582092
AN - SCOPUS:0021810190
SN - 0022-3042
VL - 45
SP - 63
EP - 72
JO - Journal of Neurochemistry
JF - Journal of Neurochemistry
IS - 1
ER -