Compartmentalized reactivity of M3/38 (anti-Mac-2) and M3/84 (anti-Mac-3) in the uterus of pregnant mice

Knisley, Keith A.; Weitlauf, Harry M.

doi:10.1530/jrf.0.0970521

Cited by 10 publications

(7 citation statements)

References 4 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…7) at M r 70,000 in liver (lane 9), placenta (lane 3), fetal membranes (lane 1), and placental-fetal membrane (lane 2); increasing total protein to 30 g revealed p70 in all tissues except kidney. 2 In conclusion, p400 is only in yolk sac, kidney, and small intestine, confirming that it is murine cubilin.…”

Section: Isolation Of Gal-3-bindingmentioning

confidence: 69%

“…large intestine; lane 13) were also negative; increasing the total protein of all tissues to 30 g again yielded negative results. 2 Immunoreactive material was observed (Fig. 7) at M r 70,000 in liver (lane 9), placenta (lane 3), fetal membranes (lane 1), and placental-fetal membrane (lane 2); increasing total protein to 30 g revealed p70 in all tissues except kidney.…”

Section: Isolation Of Gal-3-bindingmentioning

confidence: 91%

“…Incubations of 48 and 72 h or treatment with O-glycosidases or sialidases, produced no additional detectable changes. 2 Amino acid sequences of seven peptides of p400 (p400-1 through p400-7) are shown in Fig. 6A.…”

Section: Isolation Of Gal-3-bindingmentioning

confidence: 99%

“…In situ hybridization work on adjacent sections demonstrated that the cells did not contain cubilin mRNA. 2 …”

Section: Comparison Of Spatiotemporal Patterns Of Expression Of Gal-3mentioning

confidence: 99%

“…1). gal-3 and its mRNA are expressed in trophoblast cells of placenta as well as in the granular uNK cells of the metrial gland and decidualized endometrium of the murine implantation site (2)(3)(4). That finding, along with the additional observation that gal-3 is absent from nondecidualized endometrium between implantation sites and is not present in uteri of nonpregnant females (3), strongly suggests that this lectin has a pregnancy-related function at the maternalfetal interface.…”

mentioning

confidence: 99%

See 4 more Smart Citations

Cubilin, a Binding Partner for Galectin-3 in the Murine Utero-Placental Complex

Crider-Pirkle¹,

Billingsley²,

Faust³

et al. 2002

Journal of Biological Chemistry

View full text Add to dashboard Cite

Galectin-3 is a lectin important in animal development and regulatory processes and is found selectively localized at the implantation site of the mouse embryo. To better understand the role of galectin-3 at the maternal-fetal interface, a binding partner was isolated and characterized. Homogenates of uteroplacental tissue were incubated with immobilized recombinant galectin-3, and specifically bound proteins were eluted using lactose. The principal protein, p400, had an M r of 400,000 in SDS-PAGE. Physical properties of p400 and amino acid sequences of seven tryptic peptides were similar to cubilin from rats, humans, and dogs, identifying p400 as the murine ortholog of cubilin. This was further supported by the tissue distribution observed only in yolk sac, kidney, and ileum with monospecific antiserum for p400. Cubilin occurred in yolk sac epithelium throughout pregnancy, but galectin-3 was there only during the last week. Unexpectedly, cubilin was found only in perforin-containing granules of uterine natural killer (uNK) cells, although galectin-3 occurred throughout the cell cytoplasm. In situ hybridization revealed cubilin mRNA in yolk sac epithelium but not uNK cells, implying that yolk sac-derived cubilin is endocytosed by uNK cells via galectin-3. This is consistent with cubilin being an endogenous partner of galectin-3 at the maternal-fetal interface and suggests an important role for cubilin in uNK cell function. 1 is one of at least 10 members of a lectin family, which share a conserved carbohydrate recognition domain and which exert their varied biological effects through interaction with complementary ␤-galactoside ligands of glycoprotein or glycolipid "counterreceptors." Since galectins are divalent and are able to form multivalent aggregates, they can cross-link counterreceptors, effecting cell-cell, cell-matrix, or matrix-matrix interactions, thus possibly initiating signal transduction. Isolation of several membrane or matrix counterreceptors by affinity chromatography has revealed that galectins are linked to a variety of important processes including neoplastic transformation, cell adhesion, tumor invasiveness and metastasis, cellular proliferation, and localized immunomodulation (see Ref. 1). gal-3 and its mRNA are expressed in trophoblast cells of placenta as well as in the granular uNK cells of the metrial gland and decidualized endometrium of the murine implantation site (2-4). That finding, along with the additional observation that gal-3 is absent from nondecidualized endometrium between implantation sites and is not present in uteri of nonpregnant females (3), strongly suggests that this lectin has a pregnancy-related function at the maternalfetal interface. Although a role for gal-3 at the maternal-fetal interface is not yet known, it may contribute in some fashion to cell adhesion, proliferation, or immunomodulation, all of which occur in other contexts. Therefore, to gain more insight into a role for this lectin at the maternal-fetal interface, we isolated and characterized a counte...

show abstract

Section: Isolation Of Gal-3-bindingmentioning

confidence: 69%

Section: Isolation Of Gal-3-bindingmentioning

confidence: 91%

Section: Isolation Of Gal-3-bindingmentioning

confidence: 99%

“…In situ hybridization work on adjacent sections demonstrated that the cells did not contain cubilin mRNA. 2 …”

Section: Comparison Of Spatiotemporal Patterns Of Expression Of Gal-3mentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Cubilin, a Binding Partner for Galectin-3 in the Murine Utero-Placental Complex

Crider-Pirkle¹,

Billingsley²,

Faust³

et al. 2002

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

Ly6 family member C4.4A binds laminins 1 and 5, associates with galectin‐3 and supports cell migration

Paret

Bourouba

et al. 2005

Intl Journal of Cancer

View full text Add to dashboard Cite

C4.4A is a member of the Ly6 family, with low homology to uPAR. It has been detected mainly on metastasizing carcinoma cells and proposed to be involved in wound healing. So far, C4.4A has been observed as an orphan receptor, and its functional activity has not been explored. Using recombinant rat C4.4A (rrC4.4A) made in a eukaryotic expression system, we demonstrate by immunohistology that C4.4A ligands are strongly expressed in tissues adjacent to squamous epithelia of, e.g., tongue and esophagus, the expression pattern partly overlapping with laminin (LN) and complementing the C4.4A expression that is found predominantly on the basal layers of squamous epithelium. ELISA screening of several components of the extracellular matrix revealed selective binding of rrC4.4A to LN1 and LN5 and that transfection of the BSp73AS tumor line with C4.4A cDNA (BSp73AS-1B1) promoted LN1 and LN5 binding. Binding of BSp73AS-1B1 to LN5 and, less markedly, LN1 induced spreading, lamellipodia formation and migration. C4.4A also associates with galectin-3 in nontransformed tissues and tumor lines. There is evidence that the association of C4.4A with galectin-3 influences LN adhesion. C4.4A was described originally as a metastasis-associated molecule. Our findings that LN1 and LN5 are C4.4A ligands, that galectin-3 associates with C4.4A and that C4.4A ligand binding confers a migratory phenotype are well in line with the supposed metastasis association. ' 2005 Wiley-Liss, Inc.Key words: C4.4A; laminin; galectin; cell migration LNs are adhesive glycoproteins found in the basement membrane. Fifteen LN isoforms have been identified. 1 LN isoforms are tissue-specific and expressed in a developmentally regulated pattern. 2,3 Cell adhesion to LN plays an important role in maintaining normal tissue organization. LNs promote cell adhesion and migration, 4 are involved in the control of cell proliferation and gene expression 5 and stimulate neurite outgrowth, 6 the multitude of functions being brought about by a large array of receptors. 7 The most prominent LN receptors are integrins, but distinct receptors have also been described, e.g., a-dystroglycan, syndecans, the 67 kDa LN receptor and galectins. 7,8 a-Dystroglycan provides a link between the basement membrane and the dystrophin-actin cytoskeleton. 9 Its binding to LN is Ca 2þ -dependent 10 and requires carbohydrate moieties. 11 Binding of syndecans 2 and 4 to LN5 induces expression of MMP-1. 12 Moreover, syndecan 1 interacts with unprocessed LN5 in migrating keratinocytes, and this interaction depends on the presence of the glycosaminoglycan chain. 13 Galectins belong to the family of galactose-specific lectins and bind the lactosamine-type sugars on LN1. 8 However, at high concentrations, galectins 3 and 1 can downregulate adhesion to LN, probably by blocking the cellular attachment sites. 14,15 The 67 kDa LN receptor can act in concert with a6b4 to promote cell adhesion to LN1. 16 It is also involved in the degradation of LN1 and the release of motility fragments. 17 The GPI-ancho...

show abstract

Pathology Analysis of the Placenta

Bolon

2014

The Guide to Investigation of Mouse Pregnancy

View full text Add to dashboard Cite

Compartmentalized reactivity of M3/38 (anti-Mac-2) and M3/84 (anti-Mac-3) in the uterus of pregnant mice

Cited by 10 publications

References 4 publications

Cubilin, a Binding Partner for Galectin-3 in the Murine Utero-Placental Complex

Cubilin, a Binding Partner for Galectin-3 in the Murine Utero-Placental Complex

Ly6 family member C4.4A binds laminins 1 and 5, associates with galectin‐3 and supports cell migration

Pathology Analysis of the Placenta

Contact Info

Product

Resources

About