Dataset Information

Proteomics of Human Breast-TMG LC-MS/MS

ABSTRACT: Type I, II, III and V collagens were commonly identified in human, pig, and mouse breast ECM. Mammary epithelial cells were able to form acini on certain types or combinations of the four collagens at normal breast tissue stiffness levels. Comparison of the collagen species in mouse normal breast and breast tumor ECM revealed common and distinct sets of collagens within the two types of tissues. Elevated collagen type I alpha 1 chain expression was found in human breast cancers. Collagen type XXV alpha 1 chain was identified in mouse breast tumors but not in normal breast tissues. Our data provide insights into modeling human breast pathophysiological structures and functions using native tissue-derived hydrogels and potential contributions of different collagen types or their monomers in breast cancer development.

INSTRUMENT(S): Agilent instrument model

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Breast

SUBMITTER: Weimin Li

LAB HEAD: Weimin Li

PROVIDER: PXD037900 | Pride | 2023-03-11

REPOSITORIES: Pride

ACCESS DATA

Publications

Identification of the Collagen Types Essential for Mammalian Breast Acinar Structures.

Keller Chandler R CR Ruud Kelsey F KF Martinez Steve R SR Li Weimin W

Gels (Basel, Switzerland) 20221218 12

Modeling human breast tissue architecture is essential to study the pathophysiological conditions of the breast. We report that normal mammary epithelial cells grown in human breast extracellular matrix (ECM) hydrogel formed acini structurally similar to those of human and pig mammary tissues. Type I, II, III and V collagens were commonly identified in human, pig, and mouse breast ECM. Mammary epithelial cells formed acini on certain types or combinations of the four collagens at normal levels o ...[more]

PMID: 36547361

Similar Datasets

Project description:Important remodeling of the extracellular matrix is a hallmark of corneal wound healing. Besides the massive secretion of fibronectin (FN) that characterizes the early step of that process, alterations in the secretion of collagens also occurs as part of this wound healingresponse. In this study, we examined whether expression of the gene encoding the M-NM-15 subunit from the FN binding integrin M-NM-15M-NM-21 changes as corneal epithelial cells (CECs) are cultured in the presence of collagens. Responsiveness of the M-NM-15 gene toward collagen was determined by transfection of recombinant plasmids bearing the CAT reporter gene under the control of various segments from the human M-NM-15 promoter into primary cultured rabbit (RCECs) and human (HCECs) CECs cultured on BSA or on collagens. Electrophoretic mobility shift assays (EMSAs) and Western blot analyses were used to monitor both the DNA binding and expression of the transcription factors required to ensure basal transcription of the M-NM-15 gene. The influence collagens on the patterns of genes expressed by HCECs was also studied be gene profiling on microarrays. All collagen types repressed the transcriptional activity directed by the full-length M-NM-15 promoter/CAT construct in confluent CECs. A moderate increase in M-NM-15 promoter activity was observed in subconfluent RCECs grown on CIV but not on CI. These collagen-dependent regulatory influences also correlated with alterations in either the expression or the DNA binding of the transcription factors Sp1/Sp3, NFI and AP-1 that ensure basal transcription of the M-NM-15 gene. Gene profiling on microarray revealed that CI more profoundly alter the pattern of genes expressed by HCECs than what is observed with CIV. Collagens considerably suppressed expression of the M-NM-15 gene in CECs at confluence suggesting that the sustained staining for CI and CIV after corneal injury may play a role in controlling adhesion to the temporary FN matrix and further differentiation of CECs into suprabasal epithelial cells through a mechanism involving the M-NM-15M-NM-21 integrin. Primary cultures of human corneal epithelial cells cultivated on BSA (number of replicates: 2), Collagen type I (number of replicates: 2) and Collagen type IV (number of replicates: 2) matrix.

Dataset Information

Proteomics of Human Breast-TMG LC-MS/MS

Publications

Identification of the Collagen Types Essential for Mammalian Breast Acinar Structures.

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure