Laminin and type IV collagen in the human testis

Pöllänen, Pasi; Kallajoki, Markku; Risteli, Leila; Risteli, Juha; Suominen, J.

doi:10.1111/j.1365-2605.1985.tb00846.x

Cited by 38 publications

(17 citation statements)

References 17 publications

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“…The testicular vasculature also exhibited intense laminin immunostaining, especially in the muscular layer of the medium sized vessels and in the basal lamina of the endothelium. These findings are consistent with numerous approaches that investigated the localization of laminin in the testis of several mammalian species including mouse (Pelliniemi and Frojdman 2001), rat (Gelly et al 1989;El Ouali et al 1991;Pelliniemi and Frojdman 2001), dog (Benazzi et al 1995) and human (Pollanen et al 1985;Davidoff et al 1990;Santamaria et al 1990;Virtanen et al 1997;Gülkesen et al 2002;Ooba et al 2008). Taken together, the localization of laminin in the testis of mammals and birds might point out to its crucial role in the male reproduction.…”

Section: Discussionsupporting

confidence: 90%

“…Similarly, El Ouali et al (1991) identified the laminin as being expressed in Sertoli cells during rat testicular development. These data may be partially substantiated by the fact that laminin is released from cultured rat Sertoli cells (Skinner et al 1985) and is synthesized and secreted by both Sertoli and peritubular cells in human (Pollanen et al 1985;Davis et al 1990;Richardson et al 1995). The lack of laminin immunoreactivity inside the seminiferous tubules of chicken, pigeon, and rabbits may suggest that laminin protein is not translated in Sertoli cells to a sufficiently high level to be detectable by immunohistochemistry.…”

Section: Discussionmentioning

confidence: 66%

“…This interest in the seminiferous tubule extracellular matrix components stems partially from observations that overabundance of laminin is associated with an abnormally thickened lamina propria and is possibly related to male infertility (Davidoff et al 1990;Gülkesen et al 2002;Ooba et al 2008). Previously, numerous approaches have studied the localization of laminin in the testis and epididymis of several mammalian species including mouse (Pelliniemi and Frojdman 2001), rat (Gelly et al 1989;El Ouali et al 1991;Koch et al 1999;Pelliniemi and Frojdman 2001), dog (Benazzi et al 1995), human (Pollanen et al 1985;Davidoff et al 1990;Santamaria et al 1990;Virtanen et al 1997;Gülkesen et al 2002;Ooba et al 2008) and bovine (Abd-Elmaksoud 2005; Alkafafy 2005).…”

Section: Introductionmentioning

confidence: 96%

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Comparative expression of laminin and smooth muscle actin in the testis and epididymis of poultry and rabbit

Abd‐Elmaksoud

2009

J Mol Hist

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The present investigation was conducted to demonstrate laminin and alpha smooth muscle actin (alphaSMA) in the testis and epididymis of adult chickens, Sudani ducks, pigeons, and rabbits. This study may represent the first indication for the presence of laminin in the male reproductive organs of birds and rabbits and might therefore serve as a milestone for further reports. In the testis of chicken, Sudani duck, pigeon, and rabbit, the laminin was localized in the basal lamina of the seminiferous tubules and of the peritubular myoid cells, in the testicular capsule and to a small extent in the vicinity of Leydig cells. The testicular vasculature also exhibited intense laminin immunostaining. Weak laminin staining was additionally seen in the cytoplasm of the duck Sertoli cells. In the epididymis, the basal lamina of the epididymal epithelium showed a distinctly positive reaction in all birds and rabbit. The basal lamina of the periductal myoid cells also showed a positive reaction. In the interductal tissue, laminin immunostaining was particularly observed in chicken, duck and pigeon. Laminin positive reaction was also seen in the epididymal vasculatures of all birds and rabbit. Interestingly, weak to moderate laminin staining was observed in the apical surface of the ciliated cells of the proximal and distal efferent ductules in chicken, duck and pigeon. alphaSMA positive reaction was seen in the testicular capsule and in the peritubular myoid cells of all birds and rabbit. In the testicular capsule, alphaSMA staining was either observed in the inner portion (chicken) or throughout the tunica albuginea (Sudani duck and pigeon), or in the outer aspect (rabbit). Distinct alphaSMA reaction was additionally observed in the testicular vasculature. In the epididymis of all birds and rabbit, the alphaSMA was particularly seen in the periductal and interductal myoid cells as well as in the epididymal vasculatures. No alphaSMA specific staining was however detected in the epididymal epithelium, fibrous lamina propria, and luminal spermatozoa of all birds and rabbits. In conclusion, the distribution of laminin and alphaSMA in the testis and epididymis might point out to their roles in the male reproduction.

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Section: Discussionsupporting

confidence: 90%

Section: Discussionmentioning

confidence: 66%

Section: Introductionmentioning

confidence: 96%

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Comparative expression of laminin and smooth muscle actin in the testis and epididymis of poultry and rabbit

Abd‐Elmaksoud

2009

J Mol Hist

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“…The components of the extracellular matrix (ECM) of the human testis and their specific functions are not well‐known, but different collagen types, fibronectin, laminin (Pollanen et al. , 1985; Davidoff et al.…”

Section: Introductionmentioning

confidence: 99%

High levels of the extracellular matrix proteoglycan decorin are associated with inhibition of testicular function

et al. 2011

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Decorin (DCN), a component of the extracellular matrix of the peritubular wall and the interstitial areas of the human testis, can interact with growth factor (GF) signaling, thereby blocking downstream actions of GFs. In the present study the expression and regulation of DCN using both human testes and two experimental animal models, namely the rhesus monkey and mouse, were examined. DCN protein was present in peritubular and interstitial areas of adult human and monkey testes, while it was almost undetectable in adult wild-type mice. Interestingly, the levels and sites of testicular DCN expression in the monkeys were inversely correlated with testicular maturation markers. A strong DCN expression associated with the abundant connective tissue of the interstitial areas in the postnatal through prepubertal phases was observed. In adult and old monkeys the DCN pattern was similar to the one in normal human testes, presenting strong expression at the peritubular region. In the testes of both infertile men and in a mouse model of inflammation associated infertility (aromatase-overexpressing transgenic mice), the fibrotic changes and increased numbers of Tumor necrosis factor (TNF)-α-producing immune cells were shown to be associated with increased production of DCN. Furthermore, studies with human testicular peritubular cells isolated from fibrotic testis indicated that TNF-α significantly increased DCN production. The data, thus, show that an increased DCN level is associated with impaired testicular function, supporting our hypothesis that DCN interferes with paracrine signaling of the testis in health and disease.

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“…It is easily isolated and is often used to assess the biological role of ECMs, which have been shown to promote the adhesion of Sertoli cells [1], and to induce differentiation of some kinds of tumor cells [2]. The components of the seminiferous tubule extracellular matrix (ST-ECM) have been the subject of intense investigation, and the existence and/or localization of several components, such as fibronectin, laminin, entactin, SPARC, proteoglycans, and types I, III, and IV collagens have been documented [3][4][5][6][7][8][9][10][11]. However, many components of ECMs still remain to be investigated.…”

Section: Introductionmentioning

confidence: 99%

Type VI Collagen in the Rat Testis: Monoclonal Antibody, Isolation, and Localization during Development1

Sawada

Yazama

1994

Biology of Reproduction

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To investigate the components of the seminiferous tubule extracellular matrix (ST-ECM), monoclonal antibodies were raised against ST-ECM. One of these (15B6) recognized the nonreduced form of type VI collagen. With this antibody as a probe, type VI collagen was isolated from an SDS-urea extract of ST-ECM. It took a tetrameric form, and upon reduction dissociated into a major 140-kDa band and two bands at 190 and 210 kDa. Developmental changes in the distribution of type VI collagen were investigated by immunofluorescence microscopy. In 16-day rat embryos when myoid cells began to differentiate, type VI, collagen was seen in the urogenital mesentery, and it had begun to surround the gonad and, in some embryos, the seminiferous cords. In newborn rats, it was found throughout the extracellular spaces between the cords, being localized in the interstitium. In adults, however, it was confined to two parallel lines around the seminiferous tubules and to filamentous structures in the adventitia of vascular systems. Immunoelectron microscopy showed that this collagen was distributed in the interstitium independently from collagenous fibrils, but was excluded from the basal lamina of Sertoli cells. These observations indicate that type VI collagen is a major component of the ST-ECM and that it may be important in the organization of the matrix and in the differentiation of peritubular cells.

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Laminin and type IV collagen in the human testis

Cited by 38 publications

References 17 publications

Comparative expression of laminin and smooth muscle actin in the testis and epididymis of poultry and rabbit

Comparative expression of laminin and smooth muscle actin in the testis and epididymis of poultry and rabbit

High levels of the extracellular matrix proteoglycan decorin are associated with inhibition of testicular function

Type VI Collagen in the Rat Testis: Monoclonal Antibody, Isolation, and Localization during Development1

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