PATE Gene Clusters Code for Multiple, Secreted TFP/Ly-6/uPAR Proteins That Are Expressed in Reproductive and Neuron-rich Tissues and Possess Neuromodulatory Activity

Levitin, Fiana; Weiss, Mordechai; Hahn, Yoonsoo; Stern, Omer; Papke, Roger L.; Matusik, Robert J.; Nandana, Srinivas; Ziv, Ravit; Pichinuk, Edward; Salame, Sharbel; Bera, Tapan K.; Vincent, James J.; Lee, Byung Kook; Pastan, Ira; Wreschner, Daniel H.

doi:10.1074/jbc.m801454200

Cited by 54 publications

(91 citation statements)

References 35 publications

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“…For example, mammalian PATE proteins comprise a considerable group of secretory Ly-6/uPAR proteins that are mainly found in male reproductive organs. Some of these proteins have been shown to interact with nAChRs, which suggests an involvement in the modulation of neural transmission during reproduction and fertility (Levitin et al, 2008). Human SP10 and SAMP14, for example, are involved in the regulation of the sperm-egg interaction (Kong and Park, 2012), and plethodontid PMF is known to act as a courtship pheromone (Palmer et al, 2007).…”

Section: Resultsmentioning

confidence: 99%

Frog nuptial pads secrete mating season-specific proteins related to salamander pheromones

Willaert

Bossuyt

Janssenswillen

et al. 2013

Journal of Experimental Biology

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SUMMARYMales of many frog species develop spiny nuptial pads with underlying glands on their thumbs during the mating period. We used 3D visualization on the European common frog Rana temporaria to show that the morphology of these glands allows the channelling of secreted molecules to the pad's surface during amplexus. Combined transcriptome and proteome analyses show that proteins of the Ly-6/uPAR family, here termed amplexins, are highly expressed in the nuptial glands during the mating season, but are totally absent outside that period. The function of amplexins remains unknown, but it is interesting to note that they share structural similarities with plethodontid modulating factors, proteins that influence courtship duration in salamanders. Supplementary material available online at

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Section: Resultsmentioning

confidence: 99%

Frog nuptial pads secrete mating season-specific proteins related to salamander pheromones

Willaert

Bossuyt

Janssenswillen

et al. 2013

Journal of Experimental Biology

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“…PATE4 is a hypothetical prostate and testis-expressed secreted protein that has never been previously studied. Its amino acid sequence was predicted based on the sequence of its mRNA transcript (45)(46)(47).…”

Section: Discussionmentioning

confidence: 99%

Verification of Male Infertility Biomarkers in Seminal Plasma by Multiplex Selected Reaction Monitoring Assay

Drabovich

Jarvi

Diamandis

2011

Molecular & Cellular Proteomics

103

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Seminal plasma is a promising biological fluid to use for noninvasive clinical diagnostics of male reproductive system disorders. To verify a list of prospective male infertility biomarkers, we developed a multiplex selected reaction monitoring assay and measured the relative abundance of 31 proteins in 30 seminal plasma samples from normal, nonobstructive azoospermia and post-vasectomy individuals. Median levels of some proteins were decreased by more than 100-fold in nonobstructive azoospermia or post-vasectomy samples, in comparison with normal samples. To follow up the most promising candidates and measure their concentrations in seminal plasma, heavy isotope-labeled internal standards were synthesized and used to reanalyze 20 proteins in the same set of samples. Concentrations of candidate proteins in normal seminal plasma were found in the range 0.1-1000 g/ml but were significantly decreased in nonobstructive azoospermia and post-vasectomy. These data allowed us to select, for the first time, biomarkers to discriminate between normal, nonobstructive azoospermia, and post-vasectomy (simulated obstructive azoospermia) seminal plasma samples. Some testis-specific proteins (LDHC, TEX101, and SPAG11B) performed with absolute or nearly absolute specificities and sensitivities. Cell-specific classification of protein expression indicated that Sertoli or germ cell dysfunction, but not Leydig cell dysfunction, was observed in nonobstructive azoospermia seminal plasma. The proposed panel of biomarkers, pending further validation, could lead to a clinical assay that can eliminate the need for testicular biopsy to diagnose the category of male infertility, thus providing significant benefits to patients as well as decreased costs associated with the differential diagnosis of azoospermia. Molecular & Cellular Proteomics 10: 10.1074/mcp.M110.004127, 1-13, 2011.Human infertility affects ϳ15% of couples, with the male contributing to the infertility in 50% of all cases (1, 2). One of the most severe forms of male infertility is azoospermia, which is characterized by an absence of sperm in the semen (3). Azoospermia is diagnosed in 20% of subfertile men and has two forms: obstructive azoospermia (OA) 1 and nonobstructive azoospermia (NOA). OA is caused by a physical obstruction in the male reproductive tract. The biological outcome of OA is thus identical to that of vasectomy, which is a surgical severance of the vas deferens. NOA is a more complicated infertility syndrome with the azoospermia being secondary to a failure to produce sperm; NOA may be further subclassified as maturation arrest, Sertoli cell-only syndrome, and hypospermatogenesis (4).For most men with azoospermia, testicular biopsy is the only currently used method to definitively distinguish between OA and NOA (5, 6). Thus, there is an urgent need for an alternative noninvasive approach with better diagnostic potential. The differential diagnosis of normal, NOA, and OA (or post-vasectomy (PV)) men is required for the following reasons: (i) in infertile pati...

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“…Reflecting their differential expression, Ly6 proteins are used in diverse biological processes. Apart from acting as GPI-linked cell accessory proteins of the immune system, vertebrate Ly6 proteins function in the modulation of nicotinic acetylcholine receptors (Choo et al, 2008;Darvas et al, 2009;Grando, 2008;Levitin et al, 2008;Liu et al, 2009), remodelling of the extracellular matrix during skeletal muscle regeneration (Kafadar et al, 2009), self-renewal of erythroid progenitors (Bresson-Mazet et al, 2008), and lipolytic processing of triglyceride-rich lipoproteins by binding lipoprotein lipase (Beigneux et al, 2009). The presence of a GPI-anchor in Ly6 molecules, a lipid anchor that tethers the proteins on the outer leaflet of the membrane, also suggests that Ly6 proteins can aggregate in lipid rafts to alter the activity of associated proteins (Bamezai, 2004;Halova et al, 2002).…”

Section: Diverse Functions Of Ly6 Proteinsmentioning

confidence: 99%

Crooked, Coiled and Crimpled are three Ly6-like proteins required for proper localization of septate junction components

et al. 2010

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SUMMARYCellular junction formation is an elaborate process that is dependent on the regulated synthesis, assembly and membrane targeting of constituting components. Here, we report on three Drosophila Ly6-like proteins essential for septate junction (SJ) formation. SJs provide a paracellular diffusion barrier and appear molecularly and structurally similar to vertebrate paranodal septate junctions. We show that Crooked (Crok), a small GPI-anchored Ly6-like protein, is required for septa formation and barrier functions. In embryos that lack Crok, SJ components are produced but fail to accumulate at the plasma membrane. Crok is detected in intracellular puncta and acts tissue-autonomously, which suggests that it resides in intracellular vesicles to assist the cell surface localization of SJ components. In addition, we demonstrate that two related Ly6 proteins, Coiled (Cold) and Crimpled (Crim), are required for SJ formation and function in a tissue-autonomous manner, and that Cold also localizes to intracellular vesicles. Specifically, Crok and Cold are required for correct membrane trafficking of Neurexin IV, a central SJ component. The non-redundant requirement for Crok, Cold, Crim and Boudin (Bou; another Ly6 protein that was recently shown to be involved in SJ formation) suggests that members of this conserved family of proteins cooperate in the assembly of SJ components, possibly by promoting core SJ complex formation in intracellular compartments associated with membrane trafficking.

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PATE Gene Clusters Code for Multiple, Secreted TFP/Ly-6/uPAR Proteins That Are Expressed in Reproductive and Neuron-rich Tissues and Possess Neuromodulatory Activity

Cited by 54 publications

References 35 publications

Frog nuptial pads secrete mating season-specific proteins related to salamander pheromones

Frog nuptial pads secrete mating season-specific proteins related to salamander pheromones

Verification of Male Infertility Biomarkers in Seminal Plasma by Multiplex Selected Reaction Monitoring Assay

Crooked, Coiled and Crimpled are three Ly6-like proteins required for proper localization of septate junction components

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