Helena Stabile, Stefania Mitola, Emanuela Moroni, Mirella Belleri, Stefania Nicoli, Daniela Coltrini, Francesco Peri, Antonello Pessi, Laura Orsatti, Fabio Talamo, Vincent Castronovo, David Waltregny, Franco Cotelli, Domenico Ribatti, Marco Presta; Bone morphogenic protein antagonist Drm/gremlin is a novel proangiogenic factor. (B) Negative control in which the primary antibody was omitted. Bovine aortic endothelial (BAE) cells and normal subcutaneous microvascular endothelial (SIE) cells20 (both provided by A. Vecchi, Istituto Mario Negri, Milan, Italy) were cultured in DMEM supplemented with 10% heat-inactivated donor calf serum. Nano-ESI-MS/MS analysis also shows that purified Drm undergoes posttranslational modifications, including maturation, glycosylation, and phosphorylation, in keeping with previous observations in Drm-transfected COS cells.24 Indeed, purified Drm lacks the leader sequence for secretion (amino acid sequence starting from Lys-25) and carries one N-glycosylation at Asn-42 and one phosphorylation at Ser-77 (Figure 1F). After 4 days, blood vessels converging versus the implant were counted. After a PBS wash, cells were washed twice with 2.0 M NaCl in 20 mM HEPES buffer (pH 7.5) to elute 125I-rDrm bound to low-affinity sites. Ten samples of formalin-fixed and paraffin-embedded human lung cancers (5 adenocarcinomas and 5 squamous-cell carcinomas) were obtained from L. de Leval (Department of Pathology, Liège University Hospital, Belgium). The algorithm is described in the ISO 3309 standard. Alterations of blood vessel development by endothelial cells overexpressing fibroblast growth factor-2. Figure 4 Schematic representation of the gremlin 2 syntenic region in pigs. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the IntAct database. Proangiogenic activity of rDrm. Accordingly, a potent angiogenic response was observed in chick embryo CAMs implanted with Drm-transfectants when compared with mock-transfected cells (Figure S1; Table 1). Data are expressed as mean ± SD. (A) Two-dimensional electrophoresis of control and rDrm-treated SIE-cell extracts decorated with anti–phospho-Tyr antibody. The version number for both the entry and the canonical sequence are also displayed.
This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (reviewed) or to the computer-annotated TrEMBL section (unreviewed).
This section contains any relevant information that doesn't fit in any other defined sectionsOMIM database are represented with a controlled vocabulary in the following way:
This section describes post-translational modifications (PTMs) and/or processing events.
This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.
This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.
This subsection of the PTM / Processing section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).
This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.
Manually validated information inferred from a combination of experimental and computational evidence.Migrated cells at the bottom surface of the filter were stained (Diff-Quick; DADE Behring, Marburg, Germany) and counted at × 250 magnification (5 fields/sample in triplicate) using a Dialux 20 EB microscope (Leitz, Wetzlar, Germany) equipped with an NPl 25×/0.50 NA objective. Squamous tumor cells are weakly immunoreactive (A). It is updated at every UniProt release.
This section provides information on the tertiary and secondary structure of a protein.
This subsection of the 'Structure' section is used to indicate the positions of experimentally determined beta strands within the protein sequence.
This subsection of the 'Structure' section is used to indicate the positions of experimentally determined helical regions within the protein sequence.
This subsection of the 'Structure' section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence.