Sur l'Espèce humaine.

Naudin Ch. Sur l'Espèce humaine.. In: Bulletins de la Société d'anthropologie de Paris, II° Série. Tome 12, 1877. pp. 493-498

Nouvelles expériences sur l'hybridation

Naudin Ch. Nouvelles expériences sur l'hybridation. In: Bulletins de la Société d'anthropologie de Paris, II° Série. Tome 6, 1871. pp. 392-396

Remarques Au Sujet Du Croisement Suppos\ue9 Des Vari\ue9t\ue9s Blanche Et Violette Du Haricot D\u27espagne

Volume: 3Start Page: 179End Page: 18

Manuel de l'amateur des jardins : traité général d'horticulture

SignaturizadosAntepPort. con grab. xilPort. con grav. xilLas h. de grav. col. y las il. en blanco y negro intercaladas en el textoAs f. de grav. col. e as il. en br. e n. intercaladas no text

CUB-domain-containing protein 1 overexpression in solid cancers promotes cancer cell growth by activating Src family kinases

The transmembrane glycoprotein, CUB (complement C1r/C1s, Uegf, Bmp1) domain-containing protein 1 (CDCP1) is overexpressed in several cancer types and is a predictor of poor prognosis for patients on standard of care therapies. Phosphorylation of CDCP1 tyrosine sites is induced upon loss of cell adhesion and is thought to be linked to metastatic potential of tumor cells. Using a tyrosine-phosphoproteomics screening approach, we characterized the phosphorylation state of CDCP1 across a panel of breast cancer cell lines. We focused on two phospho-tyrosine pTyr peptides of CDCP1, containing Tyr707 and Tyr806, which were identified in all six lines, with the human epidermal growth factor 2-positive HCC1954 cells showing a particularly high phosphorylation level. Pharmacological modulation of tyrosine phosphorylation indicated that, the Src family kinases (SFKs) were found to phosphorylate CDCP1 at Tyr707 and Tyr806 and play a critical role in CDCP1 activity. We demonstrated that CDCP1 overexpression in HEK293 cells increases global phosphotyrosine content, promotes anchorage-independent cell growth and activates several SFK members. Conversely, CDCP1 downregulation in multiple solid cancer cell lines decreased both cell growth and SFK activation. Analysis of primary human tumor samples demonstrated a correlation between CDCP1 expression, SFK and protein kinase C (PKC) activity. Taken together, our results suggest that CDCP1 overexpression could be an interesting therapeutic target in multiple solid cancers and a good biomarker to stratify patients who could benefit from an anti-SFK-targeted therapy. Our data also show that multiple tyrosine phosphorylation sites of CDCP1 are important for the functional regulation of SFKs in several tumor types