Identification of a novel population of Langerin+ dendritic cells. J Exp Med 204: 3147-56 Chen JS, Chiu HC, Hsu CJ et al. (2009) Lowenergy visible light irradiation modulates immune responses induced by epicutaneous sensitization with protein antigen. J Invest Dermatol 129:2258-64 Isacke CM (2002) Molecules in focus the hyaluronan receptor, CD44. Int J Biochem Cell Biol 34:718-21 Merad M, Ginhoux F, Collin M (2008) Origin, homeostasis and function of Langerhans cells and other langerin-expressing dendritic cells. Nat Rev Immunol 8:935-47 Mummert DI, Takashima A, Mummert ME (2004) Langerhans cells in CD44-deficient mice emigrate from the epidermis but fail to reach the lymph nodes after hapten application. J Invest Dermatol 122:846-7 Shklovskaya E, Roediger B, Fazekas de St Groth B (2008) Epidermal and dermal dendritic cells display differential activation and migratory behavior while sharing the ability to stimulate CD4+ T cell proliferation in vivo.
Our goal was to study the prevalence of systemic sclerosis (SSc) subtypes, autoantibody profile, and pulmonary fibrosis in a large group of Han Chinese. Chinese SSc patients (n=419) were recruited from a multicenter study including hospitals and outpatient clinics in China. All patients met the American College of Rheumatology classification criteria for SSc. Anti-topoisomerase (ATA), anti-centromere (ACA), anti- RNA polymerase III (anti-RNAP3), and anti-U1- ribonucleoprotein (anti-U1RNP) were detected utilizing commercially available kits. The clinical and autoantibody information in Chinese patients was compared to that in the US Caucasian patients (n=834), recruited from the Genetics versus Environment in Scleroderma Outcome Study and Scleroderma Family Registry. Chi-square test was utilized for the abovementioned comparisons. Chinese patients showed 40.3 % limited (lcSSc) and 59.7 % diffuse (dcSSc) forms of SSc. ATA was found in 59.9 %, ACA in 13.4 %, anti-RNAP3 in 1.3 %, and anti-U1RNP in 18 % of Chinese SSc patients. Compared to US patients (65.1 % lcSSc, 34.9 % dcSSc, ATA in 18.7 %, ACA in 32.4 %, anti-RNAP3 in 17.4 %, and anti-U1RNP in 2.8 %), Chinese SSc patients are significantly higher in dcSSc and the frequencies of ATA and anti-U1RNP, but lower in ACA and anti-RNAP3. In addition, pulmonary fibrosis was observed in 78 % Chinese SSc patients and was strongly associated with the presence of ATA. The present study represents the first report of SSc features in a large group of Chinese patients. Clinical subtypes and the frequencies of SSc-related autoantibodies in Chinese SSc patients are significantly different from those in SSc patients of the US Caucasian descent.
CD69 is expressed on the surface of all hematopoietically derived leukocytes and is suggested to function as a multipurpose cell-surface trigger molecule important in the development and activation of many different cell types. Human CD69 contains only a single consensus sequence for N-linked oligosaccharide addition within its extracellular domain (Asn-Val-Thr), yet exists as two distinct glycoforms that are assembled together into disulfide-linked homodimers and heterodimers. The molecular basis for human CD69 heterogeneity has remained elusive. In the current report we show that human CD69 glycoforms are generated before the egress of CD69 proteins from the endoplasmic reticulum to the Golgi and are synthesized under conditions where Golgi processing is inhibited, effectively ruling out the possibility that CD69 heterogeneity results from the differential processing of a single glycosylation site in the Golgi complex. Importantly, these data demonstrate that contrary to current belief, not one but two sites for N-glycan addition exist within the human CD69 extracellular domain and identify the second, "cryptic" CD69 N-glycan attachment site as the atypical Cys-containing glycosylation motif, Asn-Ala-Cys. The results in this study provide a molecular basis for human CD69 heterogeneity and show that multiple dimeric forms of human CD69 result from the variable addition of N-glycans to atypical and typical glycosylation motifs within the CD69 extracellular domain.CD69 is a member of the NK gene complex family of type II oligomeric signal transmitting receptor proteins that contain C-type lectin-binding domains and is expressed on a variety of hematopoietically derived cells, including bone marrow cells, monocytes, platelets, T and B lymphocytes, and natural killer cells (1-6). In all cell types examined, CD69 cross-linking transduces intracellular signals that generate a variety of cellular responses, suggesting that CD69 is a pleiotropic immune regulator important in the biology of many different hematopoietic cell types (2, 7-9). A specific ligand for CD69 has not been identified but has been postulated to involve carbohydrate moieties (10, 11).CD69 is encoded by a single nonpolymorphic gene and is expressed in both the mouse and human as disulfide-linked homodimers and heterodimers of differentially glycosylated CD69 polypeptides or glycoforms (12-15). For mouse CD69, three putative N-glycan addition sites (Asn-X-Ser/Thr) exist within the extracellular region, accounting for the capacity to synthesize multiple CD69 glycoforms (3). Human CD69 synthesis is somewhat enigmatic in that only one N-glycan addition sequence (Asn-Val-Thr) has been identified within the extracellular domain (1, 13, 14). The molecular basis for human CD69 heterogeneity is unknown but has been proposed to result from qualititative heterogeneity in chain glycosylation, indicative of immature and mature oligosaccharides on CD69 species (2, 7). Recent studies by Hamann et al. (14) argue against this idea, however, as CD69 polypeptides synt...
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