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At least 19 recordsLinked to original sources
PubMed1979

Glycoprotein biosynthesis in calf kidney. Glycoprotein sialyltransferase activities towards serum glycoproteins and calf Tamm-Horsfall glycoprotein.

CMP-AcNeu:glycoprotein sialyltransltransltransltransltransferase of calf kidney cortex was characterized using serum glycoproteins and Tamm-Horsfall glycoprotein, obtained from calf urine, as acceptors. Native calf Tamm-Horsfall glycoprotein showed the best acceptor properties, followed by desialylated calf fetuin and desialylated human alpha 1-acid glycoprotein exhibiting V values of, respectively, 114, 63 and 41 nmol/h per g wet wt. of kidney cortex and Km values of 0.12, 0.16 and 0.26 mM glycoprotein acceptor. Desialylated ovine submaxillary mucine appeared to be a very poor acceptor. Tamm-Horsfall glycoprotein sialyltransferase could be distinguished from serum glycoprotein sialyltransferase by competition studies. In addition the two glycoprotein sialyltransferase activities showed different distributions over the three regions of the calf kidney: the ratios of the Tamm-Horsfall to serum glycoprotein sialyltransferase activities decreased from 3.3 in the cortex to 0.8 and 0.4 in the medulla and the papilla, respectively. It was concluded that in calf kidney at least two different sialyltransferases exist. The high cortical Tamm-Horsfall glycoprotein sialyltransferases activity corresponds markedly to the origin of the urinary Tamm-Horsfall glycoprotein, namely the distal part of the kidney tubule. Inactivation of glycoprotein sialyltransferase activity by preincubation at various temperatures and during storage at 0 degree C, could be reduced by the addition of CMP-AcNeu. The possible relevance towards the in vivo sialylation of this finding is discussed.

Animals↗
PubMed1995

Interaction of mouse hepatitis virus (MHV) spike glycoprotein with receptor glycoprotein MHVR is required for infection with an MHV strain that expresses the hemagglutinin-esterase glycoprotein.

In addition to the spike (S) glycoprotein that binds to carcinoembryonic antigen-related receptors on the host cell membrane, some strains of mouse coronavirus (mouse hepatitis virus [MHV]) express a hemagglutinin esterase (HE) glycoprotein with hemagglutinating and acetylesterase activity. Virions of strains that do not express HE, such as MHV-A59, can infect mouse fibroblasts in vitro, showing that the HE glycoprotein is not required for infection of these cells. The present work was done to study whether interaction of the HE glycoprotein with carbohydrate moieties could lead to virus entry and infection in the absence of interaction of the S glycoprotein with its receptor glycoprotein, MHVR. The DVIM strain of MHV expresses large amounts of HE glycoprotein, as shown by hemadsorption, acetylesterase activity, and immunoreactivity with antibodies directed against the HE glycoprotein of bovine coronavirus. A monoclonal anti-MHVR antibody, MAb-CC1, blocks binding of virus S glycoprotein to MHVR and blocks infection of MHV strains that do not express HE. MAb-CC1 also prevented MHV-DVIM infection of mouse DBT cells and primary mouse glial cell cultures. Although MDCK-I cells express O-acetylated sialic acid residues on their plasma membranes, these canine cells were resistant to infection with MHV-A59 and MHV-DVIM. Transfection of MDCK-I cells with MHVR cDNA made them susceptible to infection with MHV-A59 and MHV-DVIM. Thus, the HE glycoprotein of an MHV strain did not lead to infection of cultured murine neural cells or of nonmurine cells that express the carbohydrate ligand of the HE glycoprotein. Therefore, interaction of the spike glycoprotein of MHV with its carcinoembryonic antigen-related receptor glycoprotein is required for infectivity of MHV strains whether or not they express the HE glycoprotein.

Animals↗
PubMed1993

Effect of hypoxia on endothelial cell surface glycoprotein expression: modulation of glycoprotein IIIa and other specific surface glycoproteins.

Exposure to hypoxia alters many aspects of endothelial cell metabolism and function; however, changes in surface glycoconjugates under these conditions have not been extensively evaluated. In the current studies, we examined surface glycoproteins of cultured bovine aortic (BAEC) and pulmonary arterial (BPAEC) endothelial cells under standard culture conditions (21% oxygen) and following exposure to hypoxia (0% oxygen) for varying time periods (30 min to 18 h) using a system of biotinylation, lectin binding (concanavalin A, Con A; Griffonia simplicifolia, GSA; Arachis hypogaea, PNA; Ricinus communis, RCA; or Triticum vulgaris, WGA), subsequent strep-avidin binding, and staining. Using these methods, we identified differences in lectin binding between the two cell types cultured in 21% oxygen with all lectins except PNA. With exposure to 0% oxygen, there was no change in lectin binding to most surface glycoproteins. Several surface glycoproteins, including glycoprotein IIIa on both cell types, demonstrated a time-dependent decrease in lectin binding; in addition, there was an increase in lectin binding to a few specific surface glycoproteins on each cell type within 30-60 min of exposure to 0% oxygen. These changes in specific surface glycoproteins were confirmed in both cell types by 125I labeling. Increased lectin binding was observed for Con A binding BAEC glycoproteins at molecular weight (MW) 116, 130, and 205 kDa, GSA binding BAEC glycoproteins at MW 120 and 205 kDa, and RCA binding BPAEC glycoproteins at MW 140 and 205 kDa. Increased binding of WGA or PNA was not observed during exposure to hypoxia. The specificity of lectin binding was further confirmed by competitive inhibition with the appropriate sugar. These studies demonstrate that there are baseline differences between BAEC and BPAEC cell surface glycoproteins and that exposure to hypoxia is associated with little change in lectin binding to most surface glycoproteins. There is, however, increased surface expression of a few glycoproteins that differ depending of the origin of the endothelial cell. Although the mechanism of this increase in lectin binding is not yet clear, subsequent studies suggested that it is due to increased availability of select carbohydrate moieties. The time course of these alterations suggests a possible role in the endothelial cell response to decreases in ambient oxygen tension.

Animals↗
PubMed1998

Anti-beta 2-glycoprotein I autoantibodies from patients with the "antiphospholipid" syndrome bind to beta 2-glycoprotein I with low affinity: dimerization of beta 2-glycoprotein I induces a significant increase in anti-beta 2-glycoprotein I antibody affinity.

"Antiphospholipid" autoantibodies are associated with arterial and venous thrombosis, recurrent fetal loss, and thrombocytopenia. At present, the best-characterized antigenic target for these autoantibodies (or Abs) is the phospholipid-binding protein beta2-glycoprotein I (beta2GPI). These Abs bind beta2GPI only in the presence of negatively charged phospholipids or microtiter polystyrene plates that have been specially treated to give the surface a negative charge. To determine whether the binding of these Abs to beta2GPI on negatively charged surfaces is dependent on increased density or neo-epitopes formed as a consequence of a conformational change on beta2GPI, we generated mutants of beta2GPI by site-directed mutagenesis and assessed the binding characteristics of anti-beta2GPI Abs to these mutants. Our results demonstrate that mutant F307*, which spontaneously forms significant dimerization, is bound best by all the anti-beta2GPI Abs in an anti-beta2GPI ELISA using irradiated polystyrene microtiter plates. In addition, these Abs bound mutant F307* coated onto standard polystyrene microtiter wells in the absence of phospholipid, whereas there was minimal binding with wild-type and mutant F307*/C288A, which formed minimal dimerization. Affinity-purified anti-beta2GPI Abs from patients with the antiphospholipid syndrome demonstrated significantly higher binding affinity for mutant F307* in fluid phase than for wild-type or mutant F307*/C288A of beta2GPI. These results demonstrate that autoantibody binding to beta2GPI is intrinsically of low affinity and that the binding is dependent on the density of the Ag and not on neo-epitope formation.

Amino Acid Sequence↗
PubMed1995

Interaction of platelet glycoprotein V with glycoprotein Ib-IX regulates expression of the glycoproteins and binding of von Willebrand factor to glycoprotein Ib-IX in transfected cells.

The goal of the present study was to determine whether platelet glycoprotein (GP) V interacts directly with the von Willebrand factor receptor GP Ib-IX and, if so, whether it affects the expression and function of this receptor. A melanoma cell line that does not contain actin-binding protein was transfected with the cDNAs coding for GP V and for each of the three subunits of GP Ib-IX. GP V co-immunoprecipitated and co-localized with GP Ib-IX. Although GP V could be expressed in the absence of GP Ib-IX, the amount incorporated in the membrane was markedly increased when GP Ib-IX was present. Similarly, there was an enhanced expression of GP Ib-IX on the cell surface in the presence of GP V. The binding affinity of botrocetin-induced von Willebrand factor to GP Ib-IX was unaffected by the presence or absence of GP V. However, the binding capacity was increased by the presence of GP V. We conclude that GP V interacts directly with GP Ib-IX, that GP V must associate with GP Ib-IX to be efficiently expressed in the membrane, and that GP V increases the binding capacity of the cells for von Willebrand factor by enhancing the surface expression of the GP Ib-IX complex.

Antibodies, Monoclonal↗
PubMed1982

Nephritogenic glycoprotein. IX. Plasma Zn-alpha2-glycoprotein as a second source of nephritogenic glycoprotein in urine.

Glomerular basement membrane (GBM) damage has been considered as the only source of the nephritogenic glycoprotein excreted in urine. However, in the course of our investigation on the glycoprotein or glycopeptide isolated from the urine of a disease group seldom affected with GBM damage, it appeared that a second source of the nephritogenic glycoprotein excreted in the urine is in blood plasma; that is, in Zn-alpha2-glycoprotein. Zn-alpha2-glycoprotein is the only plasma protein which has a common determinant with nephritogenic urinary glycoprotein or glycopeptides. It was proposed that plasma Zn-alpha2-glycoprotein may play the role of a carrier protein of the nephritogenic renal glycoprotein.

Animals↗
PubMed1990

Isolation and characterization of blood group N antigen precursor glycoproteins with Thomsen-Friedenreich (T) activity, N antigen precursor glycoproteins and T-active glycoproteins from cyst fluids of malignant ovarian clear cell carcinoma.

1. Two perchloric acid-soluble glycoprotein fractions from cyst fluids of 2 patients with ovarian clear cell carcinoma in malignant were subjected to a systematic affinity chromatography using Vicia unijuga lectin-Cellulofine column and Arachis hypogaea lectin-Cellulofine column and separated into four glycoproteins, blood group N antigen precursor glycoprotein with Thomsen-Friedenreich (T) activity, N antigen precursor glycoprotein, T-active glycoprotein and serologically inactive glycoprotein, respectively. 2. These serologically active glycoproteins isolated in yields of 0.3-3.3% of PASFs, were proved to be mucin-type glycoproteins with Mw of 509,000-2,772,000 Da and contained 33.9-81.7% carbohydrates.

Acetylgalactosamine↗
PubMed1995

Presence of Vicia graminea lectin- or Vicia unijuga lectin-binding (Vgu) glycoproteins, Vgu glycoproteins with Thomsen-Friedenreich (T) activity and T-active glycoproteins in human meconium.

Perchloric acid-soluble fraction prepared from a mixture of meconiums of 22 newborn babies was subjected to a systematic affinity chromatography using Vicia unijuga lectin-Cellulofine column and Arachis hypogaea lectin-Agarose column and separated into four fractions, Vgu glycoprotein, Vgu glycoprotein with T activity, T-active glycoprotein and another glycoprotein fractions. HPLC analysis showed that the first fraction contained three glycoproteins with molecular weight (Mw) of about 19,400 kDa, 5500 kDa and 1900 kDa, the second fraction consisted of two glycoproteins with Mw of about 460 kDa and 150 kDa and the third fraction composed of several glycoproteins including the main glycoprotein with Mw of about 11,700 kDa.

Amino Acid Sequence↗
PubMed1991

Thomsen-Friedenreich (T)-active glycoproteins, blood group N antigen precursor glycoproteins and N antigen precursor glycoproteins with T activity from ascitic fluids of liver cancer patients.

1. Five perchloric acid-soluble fractions (PASFs) obtained from ascitic fluids of three patients with primary hepatocellular carcinoma (HCC), a patient with liver metastatic carcinoma (LUC) from ureteral carcinoma and human normal serum (NS) were subjected to DEAE-cellulose column chromatography to separate seven glycoprotein fractions, respectively. 2. In this chromatography, two HCC-PASFs gave a Thomsen-Friedenreich (T)-active glycoprotein, respectively. 3. Other HCC-PASF gave a T-active glycoprotein, two blood group N antigen precursor glycoproteins and an N antigen precursor glycoprotein with T activity. 4. LUC-PASF gave two T-active glycoproteins and an N antigen precursor glycoprotein with T activity. 5. NS-PASF did not give these serologically active glycoproteins.

Amino Acids↗
PubMed1985

Linkage of a membrane skeleton to integral membrane glycoproteins in human platelets. Identification of one of the glycoproteins as glycoprotein Ib.

Experiments were performed to determine whether platelets contain a membrane skeleton. Platelets were labeled by a sodium periodate/sodium [3H]borohydride method and lysed with Triton X-100. Much of the filamentous actin could be sedimented at low g forces (15,600 g, 4 min), but some of the actin filaments required high-speed centrifugation for their sedimentation (100,000 g, 3 h). The latter filaments differed from those in the low-speed pellet in that they could not be depolymerized by Ca2+ and could not be sedimented at low g forces even from Triton X-100 lysates of platelets that had been activated with thrombin. Actin-binding protein sedimented with both types of filaments, but 3H-labeled membrane glycoproteins were recovered mainly with the high-speed filaments. The primary 3H-labeled glycoprotein recovered with this "membrane skeleton" was glycoprotein (GP) Ib. Approximately 70% of the platelet GP Ib was present in this skeleton. Several other minor glycoproteins, including greater than 50% of the GP Ia and small amounts of three unidentified glycoproteins of Mr greater than 200,000, were also recovered with the membrane skeleton. The Triton X-100 insolubility of GP Ib, GP Ia, a minor membrane glycoprotein of 250,000 Mr, and actin-binding protein resulted from their association with actin filaments as they were rendered Triton X-100-soluble when actin filaments were depolymerized with deoxyribonuclease I and co-isolated with actin filaments on sucrose gradients. When isolated platelet plasma membranes were extracted with Triton X-100, actin, actin-binding protein, and GP Ib were recovered as the Triton X-100 residue. These studies show that unstimulated platelets contain a membrane skeleton composed of actin filaments and actin-binding protein that is distinct from the rest of the cytoskeleton and is attached to GP Ib, GP Ia, and a minor glycoprotein of 250,000 Mr on the plasma membrane.

Actin Cytoskeleton↗
PubMed2006

Herpes simplex virus type 1 glycoprotein L mutants that fail to promote trafficking of glycoprotein H and fail to function in fusion can induce binding of glycoprotein L-dependent anti-glycoprotein H antibodies.

The herpes simplex virus type 1 (HSV-1) glycoproteins H (gH) and L (gL) form a heterodimer and efficient expression of gH at the virion or cell surface is dependent upon gL. Five carboxy-terminal deletion mutants of gL were created and their ability to interact with and mediate cell-surface expression of gH, to promote binding of gL-dependent anti-gH antibodies and to contribute to cell fusion was analysed. All of the gL mutants bound gH, but only two mutants, containing the amino-terminal 161 or 168 aa of gL, mediated cell-surface expression of gH, and only gL161 and gL168 functioned in cell fusion. The binding of gL to gH, therefore, was not sufficient to ensure gH cell-surface expression and it was not possible to separate the gH-trafficking role of gL from gL function in fusion. Co-expression of gH with any gL mutant conferred binding of the anti-gH mAbs 53S and LP11. If the acquisition of 53S and LP11 binding to gH reflects a gL-induced conformational change, such a change is not sufficient to mediate trafficking of the gH-gL heterodimer.

Amino Acid Sequence↗
PubMed1987

Identification of an Epstein-Barr virus glycoprotein which is antigenically homologous to the varicella-zoster virus glycoprotein II and the herpes simplex virus glycoprotein B.

The Epstein-Barr virus (EBV) antigenic homologue of the varicella-zoster virus glycoprotein II and the herpes simplex virus (HSV) glycoprotein B (gB) was identified through cross-reactivity with anti-glycoprotein II and anti-glycoprotein B peptide sera. The homologue is the previously characterized EBV glycoprotein, with an apparent molecular weight of 125,000 Da, which is synthesized late during productive EBV infection and appears to be encoded by the BamHI A EBV fragment. This glycoprotein, but not other EBV proteins, reacted with the antisera in immunoprecipitation experiments and by ELISA. In addition, absorption of the sera with the purified EBV 125-kDa glycoprotein removed the cross-reacting antibody. Whether the EBV gB homologue has the same biological functions associated with HSV gB has yet to be determined.

Antigens, Viral↗
PubMed1982

Expression of type C viral glycoproteins on P815 cells: higher expression of Mr 70,000 glycoprotein-containing glycoprotein on immunogenic variants.

Cells from P815 mastocytoma, a methylcholanthrene-induced tumor, were investigated for the presence of type C viral proteins on their surface. Little or no precipitation of purified Rauscher murine leukemia virus Mr 70,000 glycoprotein was observed with sera of mice immunized with P815 cells. However, a significant precipitation was obtained with sera from syngeneic or allogeneic mice immunized with P815 tumor cell variants obtained by mutagenesis. This difference was not detected when the sera were tested for precipitation of a pure Rauscher murine leukemia virus Mr 30,000 protein. The positive sera also precipitated a Mr 90,000 glycoprotein present on the membrane of all P815 cells. This glycoprotein was shown to contain endogenous ecotropic murine leukemia virus Mr 70,000 glycoprotein. On the membrane, a separate glycoprotein with a molecular weight of 90,000 containing gag gene products was also detected with a panel of reference antibodies. The level of glycoprotein containing Mr 70,000 glycoprotein on the cell membrane of the mutagenized cell variants was higher compared to the original P815 cells. The level of expression of the glycosylated gag precursor was the same on the original P815 cells and on the mutagenized cell variants.

Animals↗
PubMed1999

Trypanosoma cruzi: monoclonal antibodies to the surface glycoprotein superfamily differentiate subsets of the 85-kDa surface glycoproteins and confirm simultaneous expression of variant 85-kDa surface glycoproteins.

Most surface glycoproteins expressed by mammalian-stage forms of Trypanosoma cruzi are homologous to the parasite's trans-sialidase and therefore are members of the parasite's trans-sialidase superfamily. Few members of this superfamily have trans-sialidase activity. The SA85-1 family is a subfamily of the trans-sialidase superfamily whose members lack trans-sialidase activity. The function of these non-trans-sialidase members remains unknown. In this report a series of monoclonal and polyclonal antibodies to the SA85-1 glycoproteins is presented. The mAbs define distinct subgroups of SA85-1 glycoproteins, and these distinct subgroups are simultaneously expressed by individual trypomastigotes, supporting previous studies indicating that multiple SA85-1 glycoproteins and trans-sialidase superfamily glycoproteins are simultaneously expressed by each trypomastigote. In addition, the antibodies define two major subsets of the SA85-1 family (subset 1 and subset 2) based on differences in migration in SDS-PAGE; the subsets do not appear to be created by differences in glycosylation. Subset 1 migrates slower and is spontaneously released or shed preferentially from the parasite surface compared to subset 2. In addition, subset 1 is attached to the trypomastigote surface by a GPI linkage. Since these glycoprotein subsets are differentially expressed, they may have different functions.

Animals↗
PubMed1990

Separation and biochemical characterization of blood group N antigen precursor glycoproteins with Thomsen-Friedenreich (T) activity, T-active glycoproteins and N antigen precursor glycoproteins from ascites of primary ovarian cancer patients.

1. Three perchloric acid-soluble fractions from ascites of three primary ovarian cancer patients were subjected to Sephacryl S-300 gel filtration, respectively, and three Fr. 1 which were eluted in the vicinity of void volume as minor fractions, were then separated by a systematic affinity chromatography using Vicia unijuga lectin-Sepharose CL-4B column and Arachis hypogaea lectin-Sepharose CL-4B column into three glycoproteins, blood group N antigen precursor glycoprotein with Thomsen-Friedenreich (T) activity, T-active glycoprotein and N antigen precursor glycoprotein, respectively. 2. These nine glycoproteins separated in yields of 0.1-1.3 mg per 100 ml of ascites, were demonstrated to be mucin-type glycoproteins with Mw of 1,791,000-4,921,000 and contained 33.8-56.1% carbohydrates.

Amino Acids↗
PubMed2001

The domains of glycoprotein D required to block apoptosis depend on whether glycoprotein D is present in the virions carrying herpes simplex virus 1 genome lacking the gene encoding the glycoprotein.

An earlier report showed that viruses lacking the open reading frames encoding glycoproteins J and D but containing the glycoprotein D in their envelopes (gD-/+ stocks) and viruses lacking both the open reading frames and the glycoproteins in their envelopes (gD-/- stocks) induce apoptosis (G. Zhou, V. Galvan, G. Campadelli-Fiume, and B. Roizman, J. Virol. 74:11782-11791, 2000). Furthermore, apoptosis was blocked by delivery in trans of genes expressing glycoprotein D or J. Whereas gD-/- stocks attach but cannot initiate productive infection, gD-/+ stocks infect cells and produce gD-/- progeny virus. The difference in the infectivity of these two stocks suggested the possibility that the requirements for blocking apoptosis may be different. To test this hypothesis, we cloned into baculoviruses the entire wild-type glycoprotein D (Bac-gD-WT), the ectodomain only (Bac-gD-A), the ectodomain and the transmembrane domain (Bac-gD-B), the ectodomain and the cytoplasmic domain without the transmembrane domain (Bac-gD-C), or the transmembrane domain and the carboxyl-terminal cytoplasmic domain (Bac-gD-D). We report the following. Apoptosis induced by gD-/+ stocks was blocked by delivery in trans of recombinant baculovirus Bac-gD-WT, Bac-gD-A, Bac-gD-B, or Bac-gD-C but not of Bac-gD. Apoptosis induced by gD-/- stocks was blocked by Bac-gD-WT or by a mixture of Bac-gD-B and Bac-gD-D but not by any baculoviruses expressing truncated glycoprotein D alone or by the mixture of Bac-gD-A and Bac-gD-D. We conclude that the requirements to block apoptosis induced by the two virus stocks are different. The gD ectodomain is sufficient to block apoptosis induced by gD, whereas both the ectodomain and the cytoplasmic domain are required to block apoptosis induced by gD-/- stocks. The results indicate that in the case of gD-/- stocks, the transmembrane domain is required either to deliver the ectodomain to the appropriate intracellular compartment or to form multimeric constructs which virtually reconstitute gD through the interaction of transmembrane domains.

Animals↗
PubMed1976

Serum glycoproteins in the liver diseases. I. Studies on sialic acid-free glycoproteins-improved competitive binding assay of desialylated glycoprotein by rat liver plasma membrane.

An improved method for quantitation of desialylated glycoproteins was developed. The assay was carried out in non-saturating condition other than saturating condition which has been used by the other authors. In the present method a lower radioactivity in the assay solution can be used. Standard curves obtained by adding an increasing amount of desialylated alpha1-acid glycoprotein to the assay solution made it possible to measure desialylated glycoproteins equivalent to 5-200 ng of desialylated alpha1-acid glycoprotein. Desialylated alpha1-acid glycoprotein used for the assay could be prepared in large scale by hydrolysis with 0.1 N-H2SO4.

Animals↗
PubMed1991

Herpes simplex virus (HSV) glycoprotein H is partially processed in a cell line that expresses the glycoprotein and fully processed in cells infected with deletion or ts mutants in the known HSV glycoproteins.

Cell lines that constitutively express herpes simplex virus 1 (HSV-1) glycoprotein H (gH-1) failed to synthesize the mature form of gH and accumulated a precursor-like form of the glycoprotein, which was retained intracellularly, most likely in RER. Fine-structure analysis of the oligosaccharides present in recombinant gH revealed oligosaccharides processed by RER enzymes; sialylated complex-type and biantennary oligosaccharides, which are assembled in the trans-Golgi, were absent. A small fraction had the characteristics of oligosaccharides processed by the early mannosidases of the Golgi. These findings suggest that a defect in the transport out of RER to the Golgi may account for the intracellular retention of the immature form of gH in cells that express the glycoprotein constitutively. Upon superinfection of cells expressing gH-1 with HSV-2, recombinant gH-1 underwent maturation, indicating that a viral function is required to attain full processing of gH. The known HSV glycoproteins do not appear to carry out this function, since in cells infected with deletion mutants in gD, gG, gE, and gE-gI, with a spontaneous gC- mutant, or with a temperature-sensitive mutant in gB, maturation of gH occurred independently of the presence or of the maturation of the single glycoproteins tested. The present findings together with previous observations on HSV, human CMV, and the EBV homologue of gH suggest that inability of gH to undergo full processing in the absence of viral protein(s) is a property of gH.

Animals↗