Two contrary functions of tenascin: Dissection of the active sites by recombinant tenascin fragments

Spring, Jürg; Beck, Konrad; Chiquet‐Ehrismann, Ruth

doi:10.1016/0092-8674(89)90294-8

Cited by 395 publications

(361 citation statements)

References 36 publications

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“…Notably, TN has been shown to inhibit cell adhesion to fibronectin (Chiquet-Ehrismann et al, 1988)' and the TN molecule has been shown to contain an anti-adhesive signal. Further investigations have shown that TN also contains a site that promotes cell adhesion (Spring et al, 1989). These properties, combined with the observations that TN is involved in the migration of cells during development of embryonic tissues and the migration of keratinocytes in skin wounds (Latijnhouwers et al, 1994), leads to speculation that the overexpression of TN in tumours may be involved in the invasion process (Riedl et al, 1995;Ishihara et al, 1995).…”

Section: Discussionmentioning

confidence: 99%

Expression of the extracellular matrix protein tenascin in malignant and benign ovarian tumours

Wilson

Langdon²,

Lessells³

et al. 1996

Br J Cancer

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Summary The extracellular matrix protein tenascin (TN) is overexpressed in a number of solid tumours. This, however, is the first study to examine TN expression in ovarian tumours. TN protein was examined in frozen sections of 50 human ovarian tumours by immunohistochemistry. Malignant and borderline tumours showed a significantly greater incidence and intensity of stromal staining than benign tumours (P<0.0001 and P=0.038 respectively). Seven omental metastases were also examined and showed a strikingly similar protein distribution to their primary tumour counterparts. The expression pattern of different RNA isoforms, created by alternative splicing of the primary transcript, was identified using reverse transcription-polymerase chain reactions (RT-PCR). The smallest TN RNA splice variant (284 bp) was found in all tumours examined, while the appearance of larger molecular weight transcripts (-490 and 556 bp), as major forms, was predominantly limited to malignant tumours, with 9/12 malignant tumours showing this pattern compared with 1/6 benign tumours. These data suggest that malignant ovarian tumours have increased expression of TN compared with benign tumours and this may be associated with induction of specific isoforms.

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Section: Discussionmentioning

confidence: 99%

Expression of the extracellular matrix protein tenascin in malignant and benign ovarian tumours

Wilson

Langdon²,

Lessells³

et al. 1996

Br J Cancer

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“…To determine which tenascin isoform was present in the tissues examined above, longitudinal sections of Day 19 chick embryo knee were processed for immunofluorescence using anti-Tn26 and anti-Tn32 monoclonal antibodies (Spring et al, 1989). Anti-Tn26 only recognizes the largest tenascin isoform, Tn230, whereas anti-Tn32 recognizes both Tn230 and Tn200.…”

Section: Tenascin Isoformsmentioning

confidence: 99%

“…When isolated in its native form, tenascin consists of six subunits associated into a disulfide-bonded "hexabrachion" structure (Vaughan et al, 1987;Erickson and Taylor, 1987). Each subunit contains a series of structural domains, including N-terminal EGF-like repeats, fibronectin type I11 repeats, and a C-terminal Ca2+-binding domain (Jones et al, 1989;Spring et al, 1989). Tenascin variants differing in molecular size have been found in both mammals and avians; they are the product of alternative splicing and differ in the number of fibronectin type I11 repeats (Spring et al, 1989;Gulcher et al, 1989;Prieto et al, 1990;Saga et al, 1991;Siri et al, 1991;Weller et al, 1991).…”

Section: Introductionmentioning

confidence: 99%

“…Each subunit contains a series of structural domains, including N-terminal EGF-like repeats, fibronectin type I11 repeats, and a C-terminal Ca2+-binding domain (Jones et al, 1989;Spring et al, 1989). Tenascin variants differing in molecular size have been found in both mammals and avians; they are the product of alternative splicing and differ in the number of fibronectin type I11 repeats (Spring et al, 1989;Gulcher et al, 1989;Prieto et al, 1990;Saga et al, 1991;Siri et al, 1991;Weller et al, 1991). In chick the largest tenascin has 13 such repeats and an Mr of 230,000 (Tn230), whereas variants with only nine or eight repeats exhibit Mr's of 200,000 (Tn200) and 190,000 (Tn190), respectively (Spring et al, 1989;Chiquet-Ehrismann et al, 1991).…”

Section: Introductionmentioning

confidence: 99%

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Tenascin is associated with articular cartilage development

Pacifici

Iwamoto

Golden

et al. 1993

Developmental Dynamics

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The roles of tenascin in cartilage development and function remain unclear. Based on the observation that tenascin is particularly abundant at the epiphyseal extremities of developing cartilaginous models of long bones in chick and mouse embryo, we tested the hypothesis that tenascin is involved in articular cartilage development. Immunofluorescence analysis revealed that tenascin was first localized in the cell condensation region of Day 4 chick embryo limb buds, where the cartilaginous models form. With further development, tenascin gene expression became indeed restricted to the articular cap of the models. Tenascin persisted in the articular cartilage of postnatal chickens but appeared to decrease with age. The protein was also abundant in embryonic and adult tracheal cartilage rings which, like articular cartilage, persist throughout postnatal life. Similar patterns of tenascin expression were seen in mouse. Using monoclonal antibodies to avian tenascin variants, we found that the bulk of articular cartilage contained the shortest tenascin variant (Tn190), whereas the largest variant (Tn230) was present in tissues associated or interacting with articular cartilage (ligaments and meniscus). The protein and its mRNA, however, were undetectable in growth plate cartilage undergoing maturation and endochondral ossification. This inverse correlation between chondrocyte maturation and tenascin production was corroborated by the finding that tenascin gene expression decreased markedly during maturation of chondrocytes in culture and during formation of a secondary ossification center within the articular cap in vivo. Thus, tenascin is intimately associated with the development of articular cartilage and other permanent cartilages whereas absence or reduced amounts of this matrix protein characterize transient cartilages which undergo maturation and are replaced by bone.0 1993 Wiley-Liss, Inc.

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“…In the chicken three variants have been characterized. These tenascin variants differ by the insertion of one or three additional fibronectin type Ill repeats into the minimal version of tenascin (Spring et a!., 1989). The different types of subunits are disulfide-linked to homo-oligomers .…”

Section: Introductionmentioning

confidence: 99%

Tenascin variants: differential binding to fibronectin and distinct distribution in cell cultures and tissues.

et al. 1991

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In the chicken, three tenascin variants have been characterized that are generated by alternative splicing of 3 of its 11 fibronectin type III repeats. Using monoclonal antibodies that react with common regions versus extra repeats of tenascin, we could distinguish and separate tenascin variants and investigate their interaction with fibronectin using multiple experimental procedures. Interestingly, in all assays used the smallest tenascin variant bound more strongly to fibronectin than the larger ones. These biochemical data were paralleled by the observation that in chick embryo fibroblast cultures only the smallest form of tenascin could be detected in the fibronectin-rich extracellular matrix network laid down by the cells. Furthermore, each tissue present in adult chicken gizzard contained a distinct set of tenascin variants. Those tissues particularly rich in extracellular matrix, such as the tendon, contained the smallest tenascin only. Intermediate-sized tenascin was present in smooth muscle, whereas the largest form was exclusively detectable underneath the epithelial lining of the villi. Thus it appears that cell type-specific forms of tenascin exist that are appropriate for the functional requirements of the respective extracellular matrices.

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Two contrary functions of tenascin: Dissection of the active sites by recombinant tenascin fragments

Cited by 395 publications

References 36 publications

Expression of the extracellular matrix protein tenascin in malignant and benign ovarian tumours

Expression of the extracellular matrix protein tenascin in malignant and benign ovarian tumours

Tenascin is associated with articular cartilage development

Tenascin variants: differential binding to fibronectin and distinct distribution in cell cultures and tissues.

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