Developmental Changes in the Basement Membrane of the Normal and Hypothyroid Postnatal Rat Testis: Segmental Localization of Fibulin-2 and Fibronectin1

Loveland, Kate L; Schlatt, Stefan; Sasaki, Takako; Chu, Mon‐Li; Timpl, Rupert; Dziadek, Marie

doi:10.1095/biolreprod58.5.1123

Cited by 33 publications

(26 citation statements)

References 54 publications

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“…This suggests a third form of molecular association, which could occur at later developmental stages and would need further examination. A transient appearance of fibulin-1 and fibulin-2 was recently shown for the basement membranes around seminiferous tubules during testis development [42]. This underscores the dynamic and versatile nature of the fibulins, whose biological functions now need to be analysed by genetic strategies.…”

Section: Discussionmentioning

confidence: 75%

Ultrastructural localization of microfibrillar fibulin-1 and fibulin-2 during heart development indicates a switch in molecular associations

Miosge¹,

Sasaki

Chu

et al. 1998

Cellular and Molecular Life Sciences (CMLS)

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The microfibrillar proteins fibulin-1 and fibulin-2 were previously identified as prominent components of the endocardial cushion tissue (ECT) during heart development and shown to persist in adult valves and septa. Immunogold staining has now been used to compare their localization in embryonic (days 9-11) and adult mouse heart with that of fibronectin and the chondroitin sulphate proteoglycan versican. All four proteins were deposited in the ECT, which consists of a hyaluronan-rich, mainly unstructured matrix, but were barely detectable in myocardial basement membranes or within endocardial cells. Digestion with hyaluronate lyase selectively released the fibulins and versican but not fibronectin from the ECT. Yet neither of the two fibulins bound to hyaluronan in solid-phase assays, in contrast to versican. In the adult heart valve, all four proteins could be detected close to cross-striated collagen fibrils or microfibrils, but only versican was lost upon exposure to hyaluronate lyase. The data indicate that fibulins are associated with the hyaluronan-matrix of ECT through a bridge of versican, but that this association changes upon valve development to another supramolecular, presumably microfibrillar organization based on fibronectin and/or fibrillins.

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Section: Discussionmentioning

confidence: 75%

Ultrastructural localization of microfibrillar fibulin-1 and fibulin-2 during heart development indicates a switch in molecular associations

Miosge¹,

Sasaki

Chu

et al. 1998

Cellular and Molecular Life Sciences (CMLS)

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“…A correlation has been found between postnatal development of testis and fibulin-2 expression in the basement membrane of seminiferous tubule in rats (11). Human ovary tissue has been shown to express high levels of fibulin-2 mRNA (30).…”

Section: Discussionmentioning

confidence: 94%

Fibulin-2 Is Dispensable for Mouse Development and Elastic Fiber Formation

Sicot¹,

Tsuda²,

Markova³

et al. 2008

Molecular and Cellular Biology

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Fibulin-2 is an extracellular matrix protein belonging to the five-member fibulin family, of which two members have been shown to play essential roles in elastic fiber formation during development. Fibulin-2 interacts with two major constituents of elastic fibers, tropoelastin and fibrillin-1, in vitro and localizes to elastic fibers in many tissues in vivo. The protein is prominently expressed during morphogenesis of the heart and aortic arch vessels and at early stages of cartilage development. To examine its role in vivo, we generated mice that do not express the fibulin-2 gene (Fbln2) through homologous recombination of embryonic stem cells. Unexpectedly, the fibulin-2-null mice were viable and fertile and did not display gross and anatomical abnormalities. Histological and ultrastructural analyses revealed that elastic fibers assembled normally in the absence of fibulin-2. No compensatory up-regulation of mRNAs for other fibulin members was detected in the aorta and skin tissue. However, in the fibulin-2 null aortae, fibulin-1 immunostaining was increased in the inner elastic lamina, where fibulin-2 preferentially localizes. The results demonstrate that fibulin-2 is not required for mouse development and elastic fiber formation and suggest possible functional redundancy between fibulin-1 and fibulin-2.

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“…They also determine the specificity of cell-matrix and cell-cell interactions, which include integrins, cadherins, and nectins [3,5]. Second are ECM proteins, which are largely glycoproteins that interact with multiple cell sur- [8,39,136] face receptors. Third are intracellular peripheral proteins, which link adhesion receptors to the underlying actin-, intermediate filament-or microtubule-based cytoskeleton [11,12].…”

Section: The Functional Unit That Confers Cell Adhesion Function In Tmentioning

confidence: 99%

Extracellular Matrix: Recent Advances on Its Role in Junction Dynamics in the Seminiferous Epithelium During Spermatogenesis1

Siu

Cheng

2004

Biology of Reproduction

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Spermatogenesis takes place in the seminiferous epithelium of the mammalian testis in which one type A1 spermatogonium (diploid, 2n) gives rise to 256 spermatids (haploid, 1n). To accomplish this, developing germ cells, such as preleptotene and leptotene spermatocytes, residing in the basal compartment of the seminiferous epithelium must traverse the blood-testis barrier (BTB) entering into the adluminal compartment for further development into round, elongating, and elongate spermatids. Recent studies have shown that the basement membrane in the testis (a modified form of extracellular matrix, ECM) is important to the event of germ cell movement across the BTB because proteins in the ECM were shown to regulate BTB dynamics via the interactions between collagens, proteases, and protease inhibitors, possibly under the regulation of cytokines. While these findings are intriguing, they are not entirely unexpected. For one, the basement membrane in the testis is intimately associated with the BTB, which represents the basolateral region of Sertoli cells. Also, Sertoli cell tight junctions (TJs) that constitute the BTB are present side-by-side with cell-cell actin-based adherens junctions (AJ, such as basal ectoplasmic specialization [ES]) and intermediate filament-based desmosome-like junctions. As such, the relative morphological layout between TJs, AJs, and desmosome-like junctions in the seminiferous epithelium is in sharp contrast to other epithelia where TJs are located at the apical portion of an epithelium or endothelium, furthest away from ECM, to be followed by AJs and desmosomes, which in turn constitute the junctional complex. For another, anchoring junctions between a cell epithelium and ECM found in multiple tissues, also known as focal contacts (or focal adhesion complex, FAC, an actin-based cell-matrix anchoring junction type), are the most efficient junction type that permits rapid junction restructuring to accommodate cell movement. It is therefore physiologically plausible, and perhaps essential, that the testis is using some components of the focal contacts to regulate rapid restructuring of AJs between Sertoli and germ INTRODUCTIONDuring spermatogenesis, preleptotene and leptotene spermatocytes residing at the basal compartment of the seminiferous epithelium adjacent to the basement membrane must traverse the blood-testis barrier (BTB) at late stage VIII through early stage IX of the epithelial cycle, entering the adluminal compartment for further development ( Figs. 1 and 2) [1][2][3]. These primary spermatocytes continue to differentiate into round, elongating, and eventually elongate spermatids while moving to the luminal edge of the epithelium and to be released into the tubule lumen at spermiation [2]. These events of cell movement across the seminiferous epithelium are also associated with extensive remodeling of actin-based cell-cell and cell-matrix anchoring junctions, also known as adherens junctions (AJs) and focal contacts, respectively; as well as intermediate filament-based ...

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Developmental Changes in the Basement Membrane of the Normal and Hypothyroid Postnatal Rat Testis: Segmental Localization of Fibulin-2 and Fibronectin1

Cited by 33 publications

References 54 publications

Ultrastructural localization of microfibrillar fibulin-1 and fibulin-2 during heart development indicates a switch in molecular associations

Ultrastructural localization of microfibrillar fibulin-1 and fibulin-2 during heart development indicates a switch in molecular associations

Fibulin-2 Is Dispensable for Mouse Development and Elastic Fiber Formation

Extracellular Matrix: Recent Advances on Its Role in Junction Dynamics in the Seminiferous Epithelium During Spermatogenesis1

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