描述：
Human Relaxin-1, also called H1 Relaxin or RLN1, is one of three human relaxins in the
structurally related insulin/relaxin superfamily. Relaxin-1 is thought to be the result of
duplication of the Relaxin-2 gene in higher primates only. In species below higher primates,
Relaxin-1 is the equivalent of human Relaxin-2. Relaxin-1 is found in some but not all tissues
expressing Relaxin-2. It is prominent in the prostate, but also present in decidua, placenta,
endometrium and at low levels in the myocardium. As with other insulin/relaxin superfamily
members, human Relaxin-1 is synthesized as a preprohormone. Processing of the 21 kDa
preproRelaxin-1 includes removal of the signal sequence, formation of two disulfide bonds
between A and B chains and removal of the intervening Cchain by a prohormone convertase.
The resulting mature protein is an unglycosylated, 6 kDa dimer of disulfidelinked A and B
chains. Human Relaxin-1 shares 76% amino acid (aa) identity with human Relaxin-2, and 43%,
50% and 43% aa identity with mouse, rat and canine Relaxin-1, respectively. An alternate
splice form of unknown significance has a 47 aa substitution which does not have typical
Cchain cleavage motifs. Relaxins confer activity by binding to leucinerich Gprotein coupled
receptors LGR7 and LGR8. Prostatic relaxins are antiapoptotic and contribute to development
and maintenance of male fertility. It is not clear whether human Relaxins -1 and -2 have distinct
functions. Both use the same receptor and have the same critical amino acids for folding and
for receptor interaction. While receptor affinity is similar, activity is lower for Relaxin-1 as
compared to Relaxin-2. Progesterone increases expression of only Relaxin-2, while
glucocorticoids increase expression of both.
原厂资料：
Human Relaxin-1, also called H1 Relaxin or RLN1, is one of three human relaxins in the
structurally related insulin/relaxin superfamily. Relaxin-1 is thought to be the result of
duplication of the Relaxin-2 gene in higher primates only. In species below higher primates,
Relaxin-1 is the equivalent of human Relaxin-2. Relaxin-1 is found in some but not all tissues
expressing Relaxin-2. It is prominent in the prostate, but also present in decidua, placenta,
endometrium and at low levels in the myocardium. As with other insulin/relaxin superfamily
members, human Relaxin-1 is synthesized as a preprohormone. Processing of the 21 kDa
preproRelaxin-1 includes removal of the signal sequence, formation of two disulfide bonds
between A and B chains and removal of the intervening Cchain by a prohormone convertase.
The resulting mature protein is an unglycosylated, 6 kDa dimer of disulfidelinked A and B
chains. Human Relaxin-1 shares 76% amino acid (aa) identity with human Relaxin-2, and 43%,
50% and 43% aa identity with mouse, rat and canine Relaxin-1, respectively. An alternate
splice form of unknown significance has a 47 aa substitution which does not have typical
Cchain cleavage motifs. Relaxins confer activity by binding to leucinerich Gprotein coupled
receptors LGR7 and LGR8. Prostatic relaxins are antiapoptotic and contribute to development
and maintenance of male fertility. It is not clear whether human Relaxins -1 and -2 have distinct
functions. Both use the same receptor and have the same critical amino acids for folding and
for receptor interaction. While receptor affinity is similar, activity is lower for Relaxin-1 as
compared to Relaxin-2. Progesterone increases expression of only Relaxin-2, while
glucocorticoids increase expression of both.
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