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Last update 08 May 2025

LMAN1

Last update 08 May 2025

Basic Info

Synonyms

ER-Golgi intermediate compartment 53 kDa protein, ERGIC-53, ERGIC53

+ [10]

Introduction

Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or both. The LMAN1-MCFD2 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins.

Drugs associated with LMAN1

Recombinant human mannose-binding lectin(NatImmune A/S)

Target

LMAN1

Mechanism

LMAN1 stimulants [+1]

Active Org.-

Originator Org.

Azanta Danmark AS

Active Indication-

Inactive Indication

Fever [+10]

Drug Highest PhaseDiscontinued

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

Clinical Trials associated with LMAN1

NCT00415311

/ TerminatedPhase 1

A Multicenter, Open-Label, Randomized, Phase 1B Study Evaluating the Safety and Tolerability of Intravenous Recombinant Human Mannose-Binding Lectin (rhMBL) in Liver Transplant Recipients

This is a multicenter, open-label, randomized, Phase 1B study evaluating liver transplant recipients receiving rhMBL (2 cohorts) or without rhMBL (1 cohort).

Start Date01 Dec 2006

Sponsor / Collaborator

Enzon Pharmaceuticals, Inc.

NCT00886496

/ WithdrawnPhase 1

A Multi-Center Study of the Safety, Tolerability, Pharmacokinetics and Dose Escalation of Intravenous Recombinant Human Mannose-Binding-Lectin (rhMBL) in MBL Deficient Pediatric Hematology/Oncology Patients With Fever and Neutropenia

RATIONALE: Recombinant human mannose-binding lectin (MBL) may be effective in preventing infection in young patients with fever and neutropenia receiving chemotherapy for blood disease or cancer.
PURPOSE: This phase I trial is studying the side effects and best dose of recombinant human mannose-binding lectin in treating young patients with MBL deficiency and fever and neutropenia.

Start Date01 Nov 2006

Sponsor / Collaborator

Enzon Pharmaceuticals, Inc.

[+1]

NCT00388999

/ CompletedPhase 1

Multi-Center,Open-Label,Randomized,Phase 1B Study Evaluating Safety & Tolerability of Intravenous rhMBL in Pts With Multiple Myeloma Receiving Melphalan-Based High-Dose Chemotherapy Followed by Autologous Hematopoietic Stem Cell Transplant

MBL deficient patients enrolled in this protocol are scheduled to be treated with melphalan-based high-dose chemotherapy followed by autologous hematopoietic stem cell transplant (HSCT) for their multiple myeloma. Patients are randomized to 0.5 mg/kg, 1.0 mg/kg, or no rhMBL.

Start Date01 Sep 2006

Sponsor / Collaborator

Enzon Pharmaceuticals, Inc.

100 Clinical Results associated with LMAN1

100 Translational Medicine associated with LMAN1

0 Patents (Medical) associated with LMAN1

298

Literatures (Medical) associated with LMAN1

01 Mar 2025·Seminars in Thrombosis and Hemostasis

Clinical, Laboratory, Molecular, and Reproductive Aspects of Combined Deficiency of Factors V and VIII

Review

Author: Yakovleva, Elena ; Zhang, Bin

AbstractCongenital combined deficiency of factor V (FV) and factor VIII (FVIII; F5F8D, OMIM 227300) is a rare hereditary coagulopathy and accounts for approximately 3% of cases of rare coagulation disorders. The prevalence of this disease in the general population is estimated to be 1:1,000,000 and is significantly higher in regions where consanguineous marriages are permitted, such as the Mideast and South Asia. The disease has an autosomal recessive mode of inheritance and therefore occurs with an equal incidence among males and females. Heterozygous mutation carriers usually do not have clinical manifestations. The molecular basis of this disease differs from that of stand-alone congenital deficiencies of FVIII and FV. F5F8D is caused by mutations in either LMAN1 or MCFD2, which encode components of a cargo receptor complex for endoplasmic reticulum to Golgi transport of FV and FVIII, leading to defects in an intracellular transport pathway shared by these two coagulation factors. Congenital combined deficiency of FV and FVIII is characterized by decreased activities of both FV and FVIII in plasma, usually to 5 to 30% of normal. Clinical manifestations in most cases are represented by mild or moderate hemorrhagic syndrome. The simultaneous decreases of two coagulation factors present complications in the diagnosis and management of the disease. In female patients, the disease requires a special approach for family planning, pregnancy management, and parturition. This review summarizes recent progress in clinical, laboratory, and molecular understanding of this disorder.

01 Feb 2025·Journal of Bioscience and Bioengineering

COP II-mediated ER-to-Golgi transport is a bottleneck for IgNAR-Fc production in the Chinese hamster ovary cell expression system

Article

Author: Omasa, Takeshi ; Lyu, Xiaofang ; Koga, Yuichi ; Yamano-Adachi, Noriko

The novel heavy-chain antibody known as immunoglobulin new antigen receptor (IgNAR) is derived from cartilaginous fishes such as sharks. IgNAR, which binds to antigens with the high specificity and affinity of a conventional IgG antibody and exhibits high resistance to denaturation, has potential as a next-generation antibody in biopharmaceutical and biotechnological applications. High-level expression of recombinant IgNAR in animal cells has been challenging. In our previous study, IgNAR was expressed as a fusion protein with a human IgG Fc region (IgNAR-Fc) in Chinese hamster ovary (CHO) cells, but did not meet the production level required for further research and application. In this study, we sought to identify the production bottleneck in CHO cells as a first step toward achieving abundant production of IgNAR. Using an established IgG high-production CHO cell line as a comparator, we found that the amounts of intracellular dimeric IgNAR-Fc produced in CHO cells were similar to those of intracellular dimeric IgG. Furthermore, the majority of intracellular IgNAR-Fc was retained in the endoplasmic reticulum (ER) and strongly colocalized to ERGIC-53, the cargo receptor for coat protein complex II (COP II)-coated vesicles. These findings suggest that COP II-mediated ER-to-Golgi transport may represent a bottleneck for IgNAR-Fc production in the CHO cell expression system.

01 Jan 2025·Proteins: Structure, Function, and Bioinformatics

Atomic visualization of flipped‐back conformations of high mannose glycans interacting with cargo lectins: An MD simulation perspective

Article

Author: Jayaprakash, Nisha Grandhi ; Sarkar, Dheeraj Kumar ; Surolia, Avadhesha

AbstractProtein–carbohydrate interactions play a crucial role in mediating several biomolecular recognition events. We attempt to unravel its intricacies by understanding how carbohydrate‐binding proteins interpret the glycan code. We aim to decipher lectin‐mediated recognition in the endoplasmic reticulum (ER), which plays a crucial role in ER‐mediated quality control (ER‐QC). The ER‐QC functions in three phases—protein folding, transport, and degradation. Altered protein QC leads to ER‐related storage disorders. Cargo transport proteins—Ergic53 and Vip36—necessary for maintaining cellular homeostasis—are our primary focus. They recognize monoglucosylated/high mannose N‐glycans on the folded glycoproteins. This article reports on the first dynamic investigation of the ER cargo lectins in complex with the high mannose glycans using an advanced sampling technique—replica exchange molecular dynamics to decipher the inherent conformational heterogeneity and the binding mechanism. The study involves simulations for the proteins complexed with three high mannose glycans—Man8B, Man9, and mono‐glucosylated glycan. The recognition process is captured using MD simulations to achieve mechanistic insights and characterize the dynamics of glycans in their native and bound states via dihedral angle analysis. Results indicate that the flipped conformation of the glycans was crucial in differentiating their interaction with the proteins. Similar conformers of the glycans are preferred for Ergic53 and Vip36 in their glycan recognition events. Ergic53 preferred Man8B while it was Man9 for Vip36, in coherence with the previous experimental reports. These simulations provide a computational microscopic purview of the mechanism at both spatial and temporal scales. The results correlate with the published experimental data on the specificities of these lectins.

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LMAN1

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