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When Glycosylation Meets Blood Cells: A Glance of the Aberrant Glycosylation in Hematological Malignancies

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Reviews of Physiology, Biochemistry and Pharmacology

Part of the book series: Reviews of Physiology, Biochemistry and Pharmacology ((REVIEWS,volume 180))

Abstract

Among neoplasia-associated epigenetic alterations, changes in cellular glycosylation have recently received attention as a key component of hematological malignancy progression. Alterations in glycosylation appear to not only directly impact cell growth and survival, but also alter the adhesion of tumor cells and their interactions with the microenvironment, facilitating cancer-induced immunomodulation and eventual metastasis. Changes in glycosylation arise from altered expression of glycosyltransferases, enzymes that catalyze the transfer of saccharide moieties to a wide range of acceptor substrates, such as proteins, lipids, and other saccharides in the endoplasmic reticulum (ER) and Golgi apparatus. Novel glycan structures in hematological malignancies represent new targets for the diagnosis and treatment of blood diseases. This review summarizes studies of the aberrant expression of glycans commonly found in hematological malignancies and their potential mechanisms and defines the specific roles of glycans as drivers or passengers in the development of hematological malignancies.

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Abbreviations

2DG:

2-Deoxy-d glucose

9-OAcSGs:

9-O-acetylated sialoglycoconjugates

Ac5GalNTGc:

Peracetyl N-thioglycolyl-d-galactosamine

aCML:

Atypical chronic myeloid leukemia

ADC:

Antibody-drug conjugate

AFP:

α-Fetoprotein

ALG9:

α-1,2-Mannosyltransferase

ALL:

Acute lymphoblastic leukemia

ALL:

Acute lymphoblastic leukemia

AML:

Acute myeloid leukemia

asialo GM2:

Gangliotriaosylceramide

Asn:

Asparagine

B-ALL:

B cell type acute lymphoblastic leukemia

B-CLL:

B cell phenotype chronic lymphocytic leukemia

BCR:

B cell antigen receptor

BL:

Burkitt lymphoma

CALR:

Calreticulin

CD138:

Cell surface proteoglycan syndecan-1

CD62L:

Lymphocyte homing receptor L-selectin

CD82 :

Kai1

CEA:

Carcinoembryonic antigen

Cer:

Ceramide

CLL:

Chronic lymphocytic leukemia

CML:

Chronic myeloid leukemia

CMML:

Chronic myelomonocytic leukemia

CNL:

Chronic neutrophilic leukemia

CSF3R:

Colony-stimulating factor-3 receptor

DLBCL:

Clinical common large B cell lymphoma

EMT:

Epithelial mesenchymal transition

ET:

Essential thrombocytosis

FL:

Follicular lymphoma

FLT3:

FMS-related tyrosine kinase 3

FNG:

Fringe glycosyltransferase

Fuc:

Fucose

GAG:

Glycosaminoglycan

Gal:

Galactose

GalNAc:

β-D-N-acetylgalactosamine

GCS:

Glucose ceramide synthase

Gg3:

Gangliotriaosylceramide

Glc:

Glucose

GlcA:

Glucuronic acid

GlcNAc:

β-D-N-acetylglucosamine

GM3:

Sialosyllactosylceramide

GPI:

Glycosyl phosphatidylinositol

GSL:

Glycosphingolipid

HCLL:

Hematopoietic cell L-selectin ligand

HER2:

Human epidermal growth factor receptor 2

HEV:

High endothelial venule

HGF:

Hepatocyte growth factor

HL:

Hodgkin’s lymphoma

HNRNPH1:

Heterogeneous nuclear ribonucleoprotein H1

HTLV-1:

T cell leukemia virus type 1

IdoA:

Iduronic acid

IFNα:

Interferon alpha

Ig VH:

Immunoglobulin variable heavy chain genes

IKKβ:

IκB kinase subunit β

ITD:

Internal tandem duplications

JMML:

Juvenile myelomonocytic leukemia

LGALS3:

Galectin-3

LSCs:

Leukemic stem cells

mAb:

Monoclonal antibody

Man:

Mannose

MDR:

Multidrug resistance

MGAT3:

Mannosyl-glycoprotein 4-β-N-acetylglucosaminyltransferase 3

MGL:

Macrophage galactose-type lectin

MM:

Multiple myeloma

MPL/TpoR:

TPO receptor

MPN:

Myeloproliferative neoplasm

MRP1:

MDR-associated protein 1

MTOG:

Mucin-type O-glycosylation

NEU3 :

Membrane type- and ganglioside-specific sialidase

Neu5Ac:

5-N-acetylneuraminic acid

non-HL:

Non-Hodgkin’s lymphoma

Pgp:

P-glycoprotein

PMF:

Primary myelofibrosis

POFUT1:

O-fucosyltransferase 1

POGLUT1/Hclp46:

O-glucosyltransferase 1

PSA:

Prostate specific antigen

PSGL1/CD162:

P-selectin glycoprotein ligand 1

PV:

Polycythemia vera

Ser:

Serine

sIgs:

Surface immunoglobulins

SNHG3:

Small nucleolar RNA host gene 3

SRGN:

Serglycin

ST3GAL1/4/5/6:

α-2,3-Sialyltransferase 1/4/5/6

ST8SIA4/6:

α-2,8-Polysialytransferase 4/6

T-ALL:

T cell type acute lymphoblastic leukemia

T-CLL:

T cell phenotype chronic lymphocytic leukemia

Thr:

Threonine

TKIs:

Tyrosine kinase inhibitors

TLRs:

Toll-like receptors

TPO:

Thrombopoietin

TrfRs:

Transferrin receptors

V regions:

Variable regions

Xyl:

Xylose

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Acknowledgement

The authors thank Dr. Huadong Liu for critical reading and English editing of the manuscript. This work was supported by the National Natural Science Foundation of China (31971053, 81770123), China Postdoctoral Science Foundation, the Scientific and Technical Foundation of Shaanxi Province (2020JM015) and the Fundamental Research Funds for the Central Universities from Xi’an Jiaotong University.

Declaration of Competing Interest: The authors declare no competing financial interests.

Author Contributions: Y. C. and X. L. conceived and designed the article frame. H. S., M. W., X. P., F. G., X. L., and Y. C. wrote the paper.

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  1. Center for Mitochondrial Biology and Medicine, The Key Laboratory of Biomedical Information Engineering of Ministry of Education, School of Life Science and Technology, Xi’an Jiaotong University, Xi’an, China

    Huining Su, Mimi Wang & Ying Cheng

  2. Key Laboratory of Resource Biology and Biotechnology Western China, College of Life Science, Northwest University, Xi’an, China

    Xingchen Pang, Feng Guan & Xiang Li

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  1. Huining Su
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Correspondence to Xiang Li or Ying Cheng .

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    Stine Helene Falsig Pedersen

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Su, H., Wang, M., Pang, X., Guan, F., Li, X., Cheng, Y. (2021). When Glycosylation Meets Blood Cells: A Glance of the Aberrant Glycosylation in Hematological Malignancies. In: Pedersen, S.H.F. (eds) Reviews of Physiology, Biochemistry and Pharmacology. Reviews of Physiology, Biochemistry and Pharmacology, vol 180. Springer, Cham. https://doi.org/10.1007/112_2021_60

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