Glucose-regulated protein precursor (GRP78) and tumor rejection antigen (GP96) are unique to hamster caput epididymal spermatozoa

Kameshwari, Duvvuri Butchi; Bhande, Satish S.; Sundaram, Curam Sreenivasacharlu; Kota, Venkatesh; Siva, Archana Bharadwaj; Shivaji, Sisinthy

doi:10.1038/aja.2010.19

Cited by 15 publications

(9 citation statements)

References 58 publications

(83 reference statements)

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“…The list of these proteins is still developing. In hamster sperm, HSPA5 and “heat shock protein 90, beta (Grp94), member 1” (HSP90B1) are caput epididymal specific, while protein disulfide isomerase associated 3 (PDIA3) is caput epididymal abundant [30]. Endoplasmic reticulum protein 29 (ERP29) is more abundant in cauda epididymal rat sperm [31].…”

Section: Discussionmentioning

confidence: 99%

“…However, HSPA5 is a surface protein of human sperm [42] and is detected in the neck region of permeabilized, ejaculated human spermatozoa [46]. On the other hand, HSPA5 is localized to the acrosome and principal piece only in caput epididymal hamster sperm during epididymal maturation [30]. In somatic cells, the expression of HSPA9 is predominant in the mitochondrial matrix [47], suggesting that HSPA9 is involved in the refolding of proteins following their transport from the cytosol into the mitochondria [48].…”

Section: Discussionmentioning

confidence: 99%

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Identification and validation of mouse sperm proteins correlated with epididymal maturation

et al. 2011

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Sperm need to mature in the epididymis to become capable of fertilization. To understand the molecular mechanisms of mouse sperm maturation, we conducted a proteomic analysis using saturation dye labeling to identify proteins of caput and cauda epididymal sperm that exhibited differences in amounts or positions on two-dimensional gels. Of eight caput epididymal sperm-differential proteins, three were molecular chaperones and three were structural proteins. Of nine cauda epididymal sperm-differential proteins, six were enzymes of energy metabolism. To validate these proteins as markers of epididymal maturation, immunoblotting and immunofluorescence analyses were performed. During epididymal transit, heat shock protein 2 was eliminated with the cytoplasmic droplet and smooth muscle γ-actin exhibited reduced fluorescence from the anterior acrosome while the signal intensity of aldolase A increased, especially in the principal piece. Besides these changes, we observed protein spots, such as glutathione S-transferase mu 5 and the E2 component of pyruvate dehydrogenase complex, shifting to more basic isoelectric points, suggesting post-translational changes such dephosphorylation occur during epididymal maturation. We conclude that most caput epididymal sperm-differential proteins contribute to the functional modification of sperm structures and that many cauda epididymal sperm-differential proteins are involved in ATP production that promotes sperm functions such as motility.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Identification and validation of mouse sperm proteins correlated with epididymal maturation

et al. 2011

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“…In a study on the hamster, five proteins were shown to increase, while 11 decreased in intensity in cauda epididymal spermatozoa. Some of the five proteins, which increased in intensity, were related to sperm metabolism and ATP production during epididymal maturation (Kameshwari et al ., ). Those that decreased could have been the result of the ubiquitin–proteasome pathway in spermatozoa as evidenced in our study.…”

Section: Selective Protein Loss In the Hermes Body: Proteasomes And Pmentioning

confidence: 97%

Dark side of the epididymis: tails of sperm maturation

et al. 2019

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Background: The Hermes body (HB) previously called the cytoplasmic droplet is a focal distension of the flagellar cytoplasm of epididymal spermatozoa consisting mainly of isolated flattened Golgi cisternae. Objective: To define a functional role for the HB of epididymal spermatozoa. Methods: Isolated fractions of HBs of epididymal spermatozoa were prepared and by quantitative tandem mass spectrometry revealed 1511 proteins. Results: The glucose transporter GLUT-3 was the most abundant protein followed by hexokinase 1, which along with the presence of all glycolytic enzymes suggested a role for the HB in glycolysis. Several TMED/p24 Golgi trafficking proteins were abundant with TMED7/p27 and TMED2/p24 defining the identity of the flattened cisternae within the HB as Golgi, along with the known Golgi proteins, GBF1, GOLPH3, Man2a1, and ManIIX. The Golgi trafficking protein TMED7/p27 via small 50-nm vesicles emanating from the Golgi cisternae was proposed to transport GLUT-3 to the plasma membrane for ATP production related to sperm motility. The internal membranes revealed abundant proteins not only of Golgi cisternae, but also of endoplasmic reticulum and endosomes. COPI and COPII coats, clathrin, SNAREs, annexins, atlastins, and GTPases were identified for vesicular trafficking and membrane fusion, in addition to ribosomes, stress proteins for protection, proteasome proteins involved in degradation, and cytoskeletal elements for migration of the HB along the flagellum. The biogenesis of the HB occurring at step 19 spermatids of the testis just prior to their release was uncovered as a key step in germ cell differentiation, where several proteins were expressed, some for the first time. Conclusion: As epididymal spermatozoa undergo remodeling of their protein makeup through selective degradation of sperm proteins during epididymal transit, then remodeling as a consequence of new protein synthesis is not excluded by our observations.

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“…Most of them have combined 2D gel electrophoresis and MS on the total extracts of immature and mature epididymal sperm from the mouse (Ijiri et al 2011), rat (Guo et al 2007), or hamster (Kameshwari et al 2010), or on subcellular compartments such as the head and flagella (Suryawanshi et al 2011), acrosomal and membranous proteins (Park et al 2012), and phosphopeptides (Baker et al 2012), or on purified sperm surface proteins (Belleannee et al 2011a). About 20 proteins involved in sperm maturation have been identified by these studies, of which only two or three have been found to be common between two studies or species.…”

Section: R31mentioning

confidence: 99%

New insights into epididymal function in relation to sperm maturation

2014

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Testicular spermatozoa acquire fertility only after 1 or 2 weeks of transit through the epididymis. At the end of this several meters long epididymal tubule, the male gamete is able to move, capacitate, migrate through the female tract, bind to the egg membrane and fuse to the oocyte to result in a viable embryo. All these sperm properties are acquired after sequential modifications occurring either at the level of the spermatozoon or in the epididymal surroundings. Over the last few decades, significant increases in the understanding of the composition of the male gamete and its surroundings have resulted from the use of new techniques such as genome sequencing, proteomics combined with high-sensitivity mass spectrometry, and gene-knockout approaches. This review reports and discusses the most relevant new results obtained in different species regarding the various cellular processes occurring at the sperm level, in particular, those related to the development of motility and egg binding during epididymal transit.

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Glucose-regulated protein precursor (GRP78) and tumor rejection antigen (GP96) are unique to hamster caput epididymal spermatozoa

Cited by 15 publications

References 58 publications

Identification and validation of mouse sperm proteins correlated with epididymal maturation

Identification and validation of mouse sperm proteins correlated with epididymal maturation

Dark side of the epididymis: tails of sperm maturation

New insights into epididymal function in relation to sperm maturation

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