Laminin α1 chain G domain peptide, RKRLQVQLSIRT, inhibits epithelial branching morphogenesis of cultured embryonic mouse submandibular gland

Kadoya, Yuichi; Nomizu, Motoyoshi; Sorokin, Lydia; Yamashina, Shohei; Yamada, Yoshihiko

doi:10.1002/(sici)1097-0177(199807)212:3<394::aid-aja7>3.0.co;2-c

Cited by 47 publications

(44 citation statements)

References 39 publications

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“…Our findings concerning the importance of cell-basement membrane interactions are consistent with previous studies establishing the importance of the basement membrane components collagen (which we suggest includes collagen IV in the basement membrane besides collagens I or III associated with mesenchyme), proteoglycans, laminin, and fibronectin in salivary gland branching morphogenesis (Grobstein and Cohen, 1965;Bernfield et al, 1972;Kadoya et al, 1998;Sakai et al, 2003). Disrupting cell interactions with the basement membrane by anti-integrin antibodies switched the morphology, migration rate, and E-cadherin localization pattern of the outer bud cells to a pattern characteristic of inner bud cells.…”

Section: Discussionsupporting

confidence: 91%

“…Because interactions involving integrin α6 and β1 subunits with laminin and other components of basement membranes are important for salivary gland branching morphogenesis (Kadoya and Yamashina, 1993;Kadoya et al, 1998;Sakai et al, 2003;Kadoya and Yamashina, 2010), we inhibited this pair of integrin subunits with monoclonal antibodies. As previously reported, inhibiting integrin function inhibited gland branching morphogenesis (Fig.…”

Section: Evaluation Of Molecular Systems Involved In Morphogenetic Epmentioning

confidence: 99%

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Region‐specific epithelial cell dynamics during branching morphogenesis

Hsu

Koo

Harunaga

et al. 2013

Developmental Dynamics

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Section: Discussionsupporting

confidence: 91%

Section: Evaluation Of Molecular Systems Involved In Morphogenetic Epmentioning

confidence: 99%

Region‐specific epithelial cell dynamics during branching morphogenesis

Hsu

Koo

Harunaga

et al. 2013

Developmental Dynamics

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“…However, the homologous 12-mer peptides of A5G77 from the ␣ 1 chain were not active. Further, the inhibition of branching morphogenesis by A5G77 resulted in a different morphology from that observed with AG73, a syndecan-binding peptide from the laminin ␣ 1 chain G domain (27). These results suggest that the EF-5 region may interact with different receptor(s), resulting in ␣ 5 chain-specific biological activity.…”

Section: Fig 2 Cell Attachment Activity Of the Ef Peptides A-c Cementioning

confidence: 80%

“…Several synthetic peptides derived from the ␣ 1 chain G domain promote heparin binding, cell adhesion, neurite outgrowth, and tumor growth and metastasis (8, 19 -21). Some of the peptides promote acinar-like formation of human salivary gland cells in culture and inhibit acinar development and lung alveolar formation in organ culture (22)(23)(24)(25)(26)(27). Many of these peptides interact with integrins or syndecan-1, a membrane-associated heparan sulfate proteoglycan (8,13,25,27,28).…”

mentioning

confidence: 99%

Biological Activities of Homologous Loop Regions in the Laminin α Chain G Domains

Suzuki

Nakatsuka

Mochizuki

et al. 2003

Journal of Biological Chemistry

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128

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Laminin ␣ chains (␣ 1 -␣ 5 chains) have diverse chainspecific biological functions. The LG4 modules of laminin ␣ chains consist of a 14-stranded ␤-sheet (A-N) sandwich structure. Several biologically active sequences have been identified in the connecting loop regions. Here, we evaluated the biological activities of the loop regions of the E and F strands in the LG4 modules using five homologous peptides from each of the mouse ␣ chains (EF-1: DYATLQLQEGRLHFMFDLG, ␣ 1 chain 2747-2765; EF-2: DFGTVQLRNGFPFFSYDLG, ␣ 2 chain 2808 -2826; EF-3: RDSFVALYLSEGHVIFALG, ␣ 3 chain 2266 -2284; EF-4: DFMTLFLAHGRLVFMFNVG, ␣ 4 chain 1511-1529; EF-5: SPSLVLFLNHGHFVAQTEGP, ␣ 5 chain 3304 -3323). These homologous peptides showed chainspecific cell attachment and neurite outgrowth activities. Well organized actin stress fibers and focal contacts with vinculin accumulation were observed in fibroblasts attached on EF-1, whereas fibroblasts on EF-2 and EF-4 showed filopodia with ruffling. Fibroblast attachment to EF-2 and EF-4 was mediated by syndecan-2. In contrast, EF-1 promoted ␣ 2 ␤ 1 integrin-mediated fibroblast attachment and inhibited fibroblast attachment to a recombinant laminin ␣ 1 chain LG4-5. The receptors for EF-3 and EF-5 are unknown. Further, when the active core sequence of EF-1 was cyclized, utilizing two additional cysteine residues at both the N and C termini through a disulfide bridge, the cyclic peptide significantly enhanced integrin-mediated cell attachment. These results indicate that integrin-mediated cell attachment to the EF-1 sequence is conformation-dependent and that the loop structure is important for the activity. The homologous peptides, which promote either integrin-or syndecan-mediated cell attachment, may be useful for understanding the cell type-and chain-specific biological activities of the laminins.

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“…5 Despite such restricted expression, crucial roles for laminin-1 in organ development and in cell differentiation have been demonstrated by cell-coating experiments, blocking antibody and antisense strategies. Several major functions have been assigned to the constitutive ␣1 chain of laminin-1, among which are the polarization of developing kidney tubules, 6,7 lung alveolar formation, 8 development of submandibular glands 9 and polarization and functional differentiation of mammary and intestinal cells. 10,11 Conversely, alterations in cell-matrix and cell-cell interactions have been shown in a number of pathologic situations, such as inflammatory processes, wound healing and malignant transformation.…”

mentioning

confidence: 99%

Overexpression of laminin ?1 chain in colonic cancer cells induces an increase in tumor growth

et al. 2001

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Laminins represent a growing family of glycoproteins constituting the basement membrane. They are known to direct many biological processes. With respect to carcinogenesis, laminins play an important role in cell adhesion, mitogenesis, differentiation and even metastasis. To further study the biological significance of laminin-1 (composed of ␣1, ␤1 and ␥1 chains) in intestinal cell differentiation or tumorigenesis, an ␣1-laminin expression vector was introduced into the HT29 colonic cancer cells, in which laminin ␣1 chain is not expressed. Upon transfection of the ␣1 chain, the ␣1␤1␥1 trimer was found secreted in the media along with free Key words: laminins; basement membrane; colonic cancer cells; tumor growth; differentiationIt is well established that in multicellular organisms, extracellular matrix molecules control various physiologic activities such as cell growth, migration, apoptosis and differentiation. The extracellular network includes the interstitial matrix and basement membranes. The basement membranes that separate the connective tissue from epithelia, muscle fibers, blood vessels and nerves are formed by a complex set of collagens and of noncollagenous glycoproteins such as laminins, nidogen and of proteoglycans, which have a unique composition in each organ. Laminins are multifunctional molecules forming a family of proteins that display organ, site and developmental specificity. 1,2 The first characterized laminin isoform, laminin-1 (composed of ␣1, ␤1 and ␥1 chains), is a crosslike-shaped molecule assembled into a triplestranded coiled-coil structure designated as the long arm. 3 As for the other extracellular matrix molecules, laminin-1 is made up of specific structural domains that allow self-assembly, permit interaction with other basement membrane molecules and encode information for the cells via specific transmembrane receptors, mostly of the integrin family. 4 Recent studies performed on various organs during development show that laminin-1 has a rather limited expression. 5 Despite such restricted expression, crucial roles for laminin-1 in organ development and in cell differentiation have been demonstrated by cell-coating experiments, blocking antibody and antisense strategies. Several major functions have been assigned to the constitutive ␣1 chain of laminin-1, among which are the polarization of developing kidney tubules, 6,7 lung alveolar formation, 8 development of submandibular glands 9 and polarization and functional differentiation of mammary and intestinal cells. 10,11 Conversely, alterations in cell-matrix and cell-cell interactions have been shown in a number of pathologic situations, such as inflammatory processes, wound healing and malignant transformation. In colorectal cancer, perturbations in the production, deposition and degradation of matrix molecules, among which are laminins, have been observed. [12][13][14][15][16] The role of laminin-1 in tumor growth and metastasis has been evaluated in several cell systems. In particular, it was shown that coinjection of puri...

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Laminin α1 chain G domain peptide, RKRLQVQLSIRT, inhibits epithelial branching morphogenesis of cultured embryonic mouse submandibular gland

Cited by 47 publications

References 39 publications

Region‐specific epithelial cell dynamics during branching morphogenesis

Region‐specific epithelial cell dynamics during branching morphogenesis

Biological Activities of Homologous Loop Regions in the Laminin α Chain G Domains

Overexpression of laminin ?1 chain in colonic cancer cells induces an increase in tumor growth

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