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  <title>NOPR Collection:</title>
  <link rel="alternate" href="http://nopr.niscpr.res.in/handle/123456789/16014" />
  <subtitle />
  <id>http://nopr.niscpr.res.in/handle/123456789/16014</id>
  <updated>2026-10-12T21:22:16Z</updated>
  <dc:date>2026-10-12T21:22:16Z</dc:date>
  <entry>
    <title>Progesterone receptors on human spermatozoa</title>
    <link rel="alternate" href="http://nopr.niscpr.res.in/handle/123456789/17136" />
    <author>
      <name>Shah, Chirag</name>
    </author>
    <author>
      <name>Modi, Deepak</name>
    </author>
    <author>
      <name>Gadkar, Sushama</name>
    </author>
    <author>
      <name>Sachdeva, Geetanjali</name>
    </author>
    <author>
      <name>Puri, Chander</name>
    </author>
    <id>http://nopr.niscpr.res.in/handle/123456789/17136</id>
    <updated>2016-07-20T04:29:34Z</updated>
    <published>2003-07-01T00:00:00Z</published>
    <summary type="text">Title: Progesterone receptors on human spermatozoa
Authors: Shah, Chirag; Modi, Deepak; Gadkar, Sushama; Sachdeva, Geetanjali; Puri, Chander
Abstract: &lt;span style="font-size:12.0pt;mso-bidi-font-size:8.0pt;&#xD;
line-height:115%;font-family:" times="" new="" roman";mso-fareast-font-family:"times="" roman";="" mso-ansi-language:en-us;mso-fareast-language:en-us;mso-bidi-language:ar-sa"=""&gt;Progesterone,&#xD;
primarily recognized as a female steroid hormone, is reported to affect several&#xD;
sperm functions especially capacitation, motility and acrosome reaction. These&#xD;
effects of progesterone on the spermatozoa are mediated via the progesterone&#xD;
bindings sites/progesterone receptor (PR) on the acrosomal membrane. These&#xD;
receptors in response to progesterone increase the intercellular Ca&lt;sup&gt;2+&lt;/sup&gt;&#xD;
levels and stimulate Ca&lt;sup&gt;&lt;span style="font-size:10.0pt;mso-bidi-font-size:&#xD;
6.0pt;line-height:115%;font-family:" times="" new="" roman";mso-fareast-font-family:="" "times="" roman";mso-ansi-language:en-us;mso-fareast-language:en-us;="" mso-bidi-language:ar-sa"=""&gt;2&lt;span style="font-size:12.0pt;mso-bidi-font-size:&#xD;
8.0pt;line-height:115%;font-family:" times="" new="" roman";mso-fareast-font-family:="" "times="" roman";mso-ansi-language:en-us;mso-fareast-language:en-us;="" mso-bidi-language:ar-sa"=""&gt;+&lt;/span&gt;&lt;/span&gt;&lt;/sup&gt;&lt;span style="font-size:12.0pt;&#xD;
mso-bidi-font-size:8.0pt;line-height:115%;font-family:" times="" new="" roman";="" mso-fareast-font-family:"times="" roman";mso-ansi-language:en-us;mso-fareast-language:="" en-us;mso-bidi-language:ar-sa"=""&gt; influx in the mature human spermatozoa via non-genomic&#xD;
mode of actions. Characterization of this receptor reveals that the sperm PR is&#xD;
masked protein and is exposed to the surface by some non-ionic detergents. Localized&#xD;
on to the acrosome region of the spermatozoa, these receptors are &lt;span style="font-size:10.0pt;mso-bidi-font-size:6.0pt;line-height:115%;font-family:&#xD;
HiddenHorzOCR;mso-hansi-font-family:" times="" new="" roman";mso-bidi-font-family:="" hiddenhorzocr;mso-ansi-language:en-us;mso-fareast-language:en-us;mso-bidi-language:="" ar-sa"=""&gt;recognized &lt;span style="font-size:12.0pt;mso-bidi-font-size:8.0pt;&#xD;
line-height:115%;font-family:" times="" new="" roman";mso-fareast-font-family:"times="" roman";="" mso-ansi-language:en-us;mso-fareast-language:en-us;mso-bidi-language:ar-sa"=""&gt;by&#xD;
most antibodies directed towards the C-terminal region of the conventional PR.&#xD;
The estimated molecular weight of PR on spermatozoa varies from 27 kDa to 85&#xD;
kDa. At the molecular level, sequences encoding for the entire DNA and hormone&#xD;
binding domains of the conventional PR are detected in the mRNA derived from&#xD;
spermatozoa. No insertions, deletions or mutations a re detected in this&#xD;
region. These results are suggestive of the fact that at least the C terminal&#xD;
region of the conventional PR is conserved in the sperm. It is hypothesized&#xD;
that post-translational modifications or peptide splicing of the conventional&#xD;
PR in spermatozoa may possibly lead to the variant of the steroid hormone&#xD;
receptor. Detailed characterization of the sperm PR will be important in&#xD;
understanding the alternate non-genomic mode of action of steroid hormone&#xD;
receptors.&lt;/span&gt;&lt;/span&gt;&lt;/span&gt;&lt;/span&gt;
Page(s): 773-780</summary>
    <dc:date>2003-07-01T00:00:00Z</dc:date>
  </entry>
  <entry>
    <title>Epididymis as a target for contraception</title>
    <link rel="alternate" href="http://nopr.niscpr.res.in/handle/123456789/17134" />
    <author>
      <name>Khole, Vrinda</name>
    </author>
    <id>http://nopr.niscpr.res.in/handle/123456789/17134</id>
    <updated>2016-07-20T04:36:10Z</updated>
    <published>2003-07-01T00:00:00Z</published>
    <summary type="text">Title: Epididymis as a target for contraception
Authors: Khole, Vrinda
Abstract: Advantage of using a vaccine based on sperm&#xD;
antigens is that it can be used both in males and females as individuals who&#xD;
have antisperm antibodies are usually infertile but otherwise healthy. Several&#xD;
sperm specific antigens identified as prospective candidates for immunocontraception&#xD;
are of testicular origin. For the purpose of immunocontraception it may be desirable&#xD;
not to disrupt spermatogenes is and testicular function. Concept of post&#xD;
testicular maturation of spermatozoa has been very well established. During&#xD;
post testicular voyage spermatozoa undergo a series of complex and sequential&#xD;
events which transforms the immature immotile spermatozoa into mature sperm.&#xD;
Acquisition of functional maturity is necessary for progressive motility, zona&#xD;
pellucida recognition culminating in sperm egg binding. Importance of&#xD;
epididymal maturation is highlighted by the fact that high percentage of male&#xD;
in fertility in human origiates from the malfunction of the epididymis. The&#xD;
epididymis has also shown to be involved in sperm storage and provides an adequate&#xD;
environment for final maturation of the sperm. It provides a conducive microenvironment&#xD;
by virtue of which the spermatozoa are protected during the storage. In view of&#xD;
this it is imperative that more attention needs to be focused on epididymal&#xD;
antigens. The information obtained will enable us to identify epididymal&#xD;
antigens relevant to fertility and also help in infertility diagnosis.
Page(s): 764-772</summary>
    <dc:date>2003-07-01T00:00:00Z</dc:date>
  </entry>
  <entry>
    <title>Embryo-endometrial proteases during early mammalian development</title>
    <link rel="alternate" href="http://nopr.niscpr.res.in/handle/123456789/17132" />
    <author>
      <name>Seshagiri, P B</name>
    </author>
    <author>
      <name>Lalitha, H S</name>
    </author>
    <author>
      <name>Mishra, A</name>
    </author>
    <author>
      <name>Sireesha, G V</name>
    </author>
    <id>http://nopr.niscpr.res.in/handle/123456789/17132</id>
    <updated>2016-07-20T04:31:39Z</updated>
    <published>2003-07-01T00:00:00Z</published>
    <summary type="text">Title: Embryo-endometrial proteases during early mammalian development
Authors: Seshagiri, P B; Lalitha, H S; Mishra, A; Sireesha, G V
Abstract: &lt;span style="font-size:14.0pt;line-height:&#xD;
115%;font-family:" times="" new="" roman";mso-fareast-font-family:"times="" roman";="" mso-ansi-language:en-in;mso-fareast-language:en-in;mso-bidi-language:hi"="" lang="EN-IN"&gt;In&#xD;
mammals, extensive remodeling of uterine endometrial matrix occurs during&#xD;
reproductive cycle and blastocyst implantation. This is regulated by a variety&#xD;
of molecules such as hormones, growth factors, cytokines and proteases. In this&#xD;
article, we review the current state or knowledge available on various proteases&#xD;
and their inhibitors functionally involved in the embryo-endometrial tissues&#xD;
and present some data on endometrial proteases in hamsters and rats during&#xD;
estrous cycle and early pregnancy. We demonstrate the presence of at least four&#xD;
gelat inolytic activities in endometrial samples, belonging to gelatinase-A and&#xD;
-B categories and their dependence on calcium/zinc ions for enzyme activity and,&#xD;
their interrelationships between zymogen and active forms. We believe that the&#xD;
embryo-endometrial proteases are essential for hatching or blastocysts and for&#xD;
the dynamic remodeling of endometrial tissue occurring during the critical peri&#xD;
implantation period.&lt;/span&gt;
Page(s): 756-763</summary>
    <dc:date>2003-07-01T00:00:00Z</dc:date>
  </entry>
  <entry>
    <title>Expression and regulation of integrin receptors in human trophoblast cells: Role of estradiol and cytokines</title>
    <link rel="alternate" href="http://nopr.niscpr.res.in/handle/123456789/17130" />
    <author>
      <name>Das, Chandana</name>
    </author>
    <author>
      <name>Basak, Sayantani</name>
    </author>
    <id>http://nopr.niscpr.res.in/handle/123456789/17130</id>
    <updated>2016-07-20T04:35:21Z</updated>
    <published>2003-07-01T00:00:00Z</published>
    <summary type="text">Title: Expression and regulation of integrin receptors in human trophoblast cells: Role of estradiol and cytokines
Authors: Das, Chandana; Basak, Sayantani
Abstract: &lt;span style="font-size:14.0pt;line-height:&#xD;
115%;font-family:" times="" new="" roman";mso-fareast-font-family:"times="" roman";="" mso-ansi-language:en-in;mso-fareast-language:en-in;mso-bidi-language:hi"="" lang="EN-IN"&gt;Embryo&#xD;
implantation and placentation are dynamic cellular events that require not only&#xD;
synchrony between the maternal environment and the embryo, but also complex&#xD;
cell-cell communication amongst the implanting blastocyst and the receptive endomatrium&#xD;
through integrins, a large family of proteins involved in the attatchment,&#xD;
migration, invasion and control of cellular functions. Integrins display&#xD;
dynamic temporal and spatial patterns of expression by the trophoblast cells&#xD;
during early pregnancy in humans. However, the precise mechanism of embryo&#xD;
implantation and the modulation of the integrin receptors during blastocyst&#xD;
attachment and further implantation remin elusive in the humans. The present&#xD;
study elucidates the expression and hormonal modulation of fibronectin, vitronectin&#xD;
and laminin integrin receptors by estradiol and IL-1α in human trophoblast&#xD;
cells. Human first trimester trophoblast cells showed the induction of the&#xD;
classical estrogen receptor (ER)-α by its own ligand ,estradiol. Treatment with&#xD;
either estradiol or IL-&#xD;
1α induced the expressions of α&lt;sub&gt;4&lt;/sub&gt;α&lt;sub&gt;5&lt;/sub&gt;α&lt;sub&gt;6&lt;/sub&gt; and α&lt;sub&gt;v&lt;/sub&gt;,&#xD;
integrin receptor subunits at both the mRNA and protein levels, while expression&#xD;
of β&lt;sub&gt;1&lt;/sub&gt; remained unaltered. Furthermore estradiol upregulated the&#xD;
expression of IL- 1α, thereby suggesting the possibility that estrogen may either&#xD;
directly or via the proinflammatory cytokine induces the expression of the cell&#xD;
surface integrin receptors. The findings delineate the role of hormones and the&#xD;
cytokines in modulating the adhesiveness and attatchment of the trophoblast&#xD;
cells. This may reflect the &lt;i&gt;in vivo&lt;/i&gt; scenario where the implanting embryo&#xD;
is surrounded by a hormone-cytokine rich uterine microenvironment that may preisely&#xD;
regulate the expression of integrins and thereby facilitate implantation.&lt;/span&gt;
Page(s): 748-755</summary>
    <dc:date>2003-07-01T00:00:00Z</dc:date>
  </entry>
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