Study review of camelid and shark antibodies for biomedical and biotechnological applications

The antibodies of camelids and sharks are about one–half of the conventional ones while regular antibodies have four protein chains: two light and two heavy, these small antibodies studied have just two heavy chains; they lack a light chain. In recent years, nanobodies have been the focus of attention because they can recognize epitopes that are usually not antigenic (hidden) for conventional antibodies. On the clinical side, researchers are testing nanobodies (Nbs) in the fight against diseases and disease diagnosis. Nanobodies also are attractive because they can prevent protein aggregation and clear the already existing aggregates. Furthermore, new treatments using these Nbs can neutralize the severe acute respiratory syndrome coronavirus (SARS-CoV-2) for preventing COVID-19. In this review, we sum up recent findings of the proposed nanobodies for their potential application.

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Prediagnostic Neurofilament Light Chain Levels in Amyotrophic Lateral Sclerosis

Neurology ◽

10.1212/wnl.0000000000012632 ◽

2021 ◽

pp. 10.1212/WNL.0000000000012632

Author(s):

Kjetil Bjornevik ◽

Eilis J. O'Reilly ◽

Samantha Molsberry ◽

Laurence N. Kolonel ◽

Loic Le Marchand ◽

...

Keyword(s):

Light Chain ◽

Conditional Logistic Regression ◽

Disease Diagnosis ◽

Health Study ◽

Plasma Samples ◽

Blood Draw ◽

Neurofilament Light Chain ◽

Neurofilament Light ◽

Rate Ratios

Objective:To assess whether plasma neurofilament light chain (NfL) levels are elevated before ALS diagnosis and to evaluate whether pre-diagnostic NfL levels are associated with metabolic alterations.Methods:We conducted a matched case-control study nested in three large prospective US cohorts (the Nurses’ Health Study, the Health Professionals Follow-up Study, and the Multiethnic Cohort Study), and identified 84 individuals who developed ALS during follow-up and had available plasma samples prior to disease diagnosis. For each ALS case, we randomly selected controls from those who were alive at the time of the case diagnosis and matched on birth year, sex, race/ethnicity, fasting status, cohort, and time of blood draw. We measured NfL in the plasma samples and used conditional logistic regression to estimate rate ratios (RRs) and 95% confidence intervals (CIs) for ALS, adjusting for body mass index, smoking, physical activity, and urate levels.Results:Higher NfL levels were associated with a higher ALS risk in plasma samples collected within 5 years of the ALS diagnosis (RR per 1 standard deviation [SD] increase: 2.68, 95% CI: 1.18-6.08), but not in samples collected further away from the diagnosis (RR per 1 SD increase 1.16, 95% CI: 0.78-1.73). A total of 21 metabolites were correlated with pre-diagnostic NfL levels in ALS cases (p < 0.05), but none of these remained significant after multiple comparison adjustments.Conclusions:Plasma NfL levels were elevated in pre-diagnostic ALS cases, indicating that NfL may be a useful biomarker already in the earliest stages of the disease.Classification of Evidence:This study provides Class II evidence that plasma NfL levels are elevated in pre-diagnostic ALS patients.

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Neuropathological and biochemical investigation of Hereditary Ferritinopathy cases with ferritin light chain mutation: Prominent protein aggregation in the absence of major mitochondrial or oxidative stress

Neuropathology and Applied Neurobiology ◽

10.1111/nan.12634 ◽

2020 ◽

Author(s):

M. Kurzawa‐Akanbi ◽

M. Keogh ◽

E. Tsefou ◽

L. Ramsay ◽

M. Johnson ◽

...

Keyword(s):

Oxidative Stress ◽

Protein Aggregation ◽

Light Chain ◽

Biochemical Investigation

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Regulatory Light Chain-a Myosin Kinase (aMK) Catalyzes Phosphorylation of Smooth Muscle Myosin Heavy Chains of Scallop, Patinopecten yessoensis

The Journal of Biochemistry ◽

10.1093/oxfordjournals.jbchem.a122578 ◽

1988 ◽

Vol 104 (6) ◽

pp. 889-893 ◽

Cited By ~ 13

Author(s):

Hitoshi Sohma ◽

Hirohiko Sasada ◽

Kaoru Inoue ◽

Fumi Morita

Keyword(s):

Smooth Muscle ◽

Light Chain ◽

Regulatory Light Chain ◽

Smooth Muscle Myosin ◽

Myosin Heavy Chains ◽

Patinopecten Yessoensis ◽

Heavy Chains ◽

Muscle Myosin

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Effects of unweighting and clenbuterol on myosin light and heavy chains in fast and slow muscles of rat

AJP Cell Physiology ◽

10.1152/ajpcell.2000.279.5.c1558 ◽

2000 ◽

Vol 279 (5) ◽

pp. C1558-C1563 ◽

Cited By ~ 72

Author(s):

Laurence Stevens ◽

Carole Firinga ◽

Bärbel Gohlsch ◽

Bruno Bastide ◽

Yvonne Mounier ◽

...

Keyword(s):

Light Chain ◽

Extensor Digitorum Longus ◽

Extensor Digitorum ◽

Hindlimb Suspension ◽

Adrenergic Agonist ◽

Heavy Chains ◽

Fast And Slow Muscles ◽

Induced Changes ◽

Fast Muscles ◽

Slow And Fast Muscles

To investigate the plasticity of slow and fast muscles undergoing slow-to-fast transition, rat soleus (SOL), gastrocnemius (GAS), and extensor digitorum longus (EDL) muscles were exposed for 14 days to 1) unweighting by hindlimb suspension (HU), or 2) treatment with the β2-adrenergic agonist clenbuterol (CB), or 3) a combination of both (HU-CB). In general, HU elicited atrophy, CB induced hypertrophy, and HU-CB partially counteracted the HU-induced atrophy. Analyses of myosin heavy (MHC) and light chain (MLC) isoforms revealed HU- and CB-induced slow-to-fast transitions in SOL (increases of MHCIIa with small amounts of MHCIId and MHCIIb) and the upregulation of the slow MHCIa isoform. The HU- and CB-induced changes in GAS consisted of increases in MHCIId and MHCIIb (“fast-to-faster transitions”). Changes in the MLC composition of SOL and GAS consisted of slow-to-fast transitions and mainly encompassed an exchange of MLC1s with MLC1f. In addition, MLC3f was elevated whenever MHCIId and MHCIIb isoforms were increased. Because the EDL is predominantly composed of type IID and IIB fibers, HU, CB, and HU-CB had no significant effect on the MHC and MLC patterns.

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Fate of surrogate light chains in B lineage cells.

Journal of Experimental Medicine ◽

10.1084/jem.183.2.421 ◽

1996 ◽

Vol 183 (2) ◽

pp. 421-429 ◽

Cited By ~ 38

Author(s):

K Lassoued ◽

H Illges ◽

K Benlagha ◽

M D Cooper

Keyword(s):

B Cells ◽

Cell Surface ◽

Light Chain ◽

Light Chains ◽

Receptor Complex ◽

Surrogate Light Chain ◽

Heavy Chains ◽

Receptor Component ◽

B Lineage ◽

Receptor Assembly

Biosynthesis of the immunoglobulin (Ig) receptor components and their assembly were examined in cell lines representative of early stages in human B lineage development. In pro-B cells, the nascent surrogate light chain proteins form a complex that transiently associates in the endoplasmic reticulum with a spectrum of unidentified proteins (40, 60, and 98 kD) and Bip, a heat shock protein family member. Lacking companion heavy chains, the surrogate light chains in pro-B cells do not associate with either the Ig(alpha) or Ig(beta) signal transduction units, undergo rapid degradation, and fail to reach the pro-B cell surface. In pre-B cells, by contrast, a significant portion of the surrogate light chain proteins associate with mu heavy chains, Ig(alpha), and Ig(beta) to form a stable receptor complex with a relatively long half-life. Early in this assembly process, Bip/GRP78, calnexin, GRP94, and a protein of approximately 17 kD differentially bind to the nascent mu heavy chains. The 17-kD intermediate is gradually replaced by the surrogate light chain protein complex, and the Ig(alpha) and Ig(beta) chains bind progressively to the mu heavy chains during the complex and relatively inefficient process of pre-B receptor assembly. The results suggest that, in humans, heavy chain association is essential for surrogate light chain survival and transport to the cell surface as an integral receptor component.

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Light-chain only multiple myeloma is due to the absence of functional (productive) rearrangement of the IgH gene at the DNA level

Blood ◽

10.1182/blood-2003-07-2501 ◽

2004 ◽

Vol 103 (10) ◽

pp. 3869-3875 ◽

Cited By ~ 17

Author(s):

Florence Magrangeas ◽

Marie-Laure Cormier ◽

Géraldine Descamps ◽

Nadège Gouy ◽

Laurence Lodé ◽

...

Keyword(s):

Multiple Myeloma ◽

Light Chain ◽

Fluorescent In Situ Hybridization ◽

Myeloma Cell ◽

Monoclonal Immunoglobulin ◽

Heavy Chains ◽

B Cell Maturation ◽

Switch Regions ◽

Igh Rearrangement

Abstract Although most multiple myeloma (MM) cases are characterized by the detection of a monoclonal immunoglobulin in the serum, about 15% of the patients present only immunoglobulin light chains, detected either in the urine or serum or both. These patients are designated as having light-chain (LC) MM. Using fiber-fluorescent in situ hybridization, and in contrast to patients and myeloma cell lines secreting heavy chains (who presented a legitimate functional IgH rearrangement in every case), LC MM never displayed a functional IgH recombination. Interestingly, most LC MM cases presented one IgH allele with a germline configuration (including the DJ region), the second allele being usually involved in an illegitimate recombination. Of note, most of these translocations occurred close to (or at) switch regions, even though in some cases, breakpoints involving nonswitch regions were observed. Thus, this study clearly showed that LC MM is due to the absence of legitimate IgH rearrangement at the DNA level, reflecting possible abnormalities in the IgH gene recombinations during B-cell maturation. Furthermore, it showed that this defect did not prevent the activation of the switch process because most of 14q32 translocations observed in LC MM occurred at switch regions.

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Relative synthesis of cardiac contractile proteins. Evidence for synthesis from the same precursor pool

Biochemical Journal ◽

10.1042/bj1940673 ◽

1981 ◽

Vol 194 (3) ◽

pp. 673-678 ◽

Cited By ~ 11

Author(s):

C D Evans ◽

S S Schreiber ◽

M Oratz ◽

M A Rothschild

Keyword(s):

Light Chain ◽

Contractile Proteins ◽

Light Chains ◽

Myosin Heavy Chains ◽

Perfused Heart ◽

Precursor Pool ◽

Heavy Chains ◽

Cardiac Contractile ◽

Specific Activities ◽

Cardiac Contractile Proteins

The relative molar synthesis of cardiac contractile proteins has been measured in the perfused heart under control haemodynamic conditions. This synthesis, of myosin heavy chains, individual light chains (1 and 2), actin and tropomyosin, was determined from isolated guinea-pig hearts perfused for 3h simultaneously with constant specific radioactivities and concentrations of [3H]lysine and [3H]phenylalanine.The data strongly suggest that all of the proteins studied were synthesized from the same precursor pools of lysine and phenylalanine, since the ratio of the specific activities of the two labels was the same in all of the proteins. Measurement of molar synthesis of each contractile protein was the same with either labelled amino acid. Under control haemodynamic-perfusion conditions, the relative molar synthesis of the contractile proteins was actin greater than heavy chains greater than light chain 2 greater than light chain 1 greater than tropomyosin.

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Properties of the non-specific calcium-binding sites of rabbit skeletal-muscle myosin

Biochemical Journal ◽

10.1042/bj1850265 ◽

1980 ◽

Vol 185 (1) ◽

pp. 265-268 ◽

Cited By ~ 10

Author(s):

J Wikman-Coffelt

Keyword(s):

Skeletal Muscle ◽

Light Chain ◽

Binding Sites ◽

Calcium Binding ◽

Light Chains ◽

Binding Properties ◽

Skeletal Muscle Myosin ◽

Heavy Chains ◽

Calcium Binding Sites ◽

Muscle Myosin

The non-specific Ca2+-binding sites of skeletal-muscle myosin are located on the light chains; with the dissociation of light chains there is a corresponding decrease in the number of Ca2+-binding sites on light-chain-deficient myosin. The released light chains have a decreased binding affinity. Myosin heavy chains indirectly influence the Ca2+-binding properties of light chains by increasing the affinity of light chains for bivalent cations; this influence varies with pH. Because of light-chain dissociation at low Ca2+ and/or Mg2+ concentrations, anomalies may exist when analyses of non-specific Ca2+-binding properties of myosin are assessed by dialysis equilibrium.

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Axonemal dynein light chain-1 locates at the microtubule-binding domain of the γ heavy chain

Molecular Biology of the Cell ◽

10.1091/mbc.e15-05-0289 ◽

2015 ◽

Vol 26 (23) ◽

pp. 4236-4247 ◽

Cited By ~ 14

Author(s):

Muneyoshi Ichikawa ◽

Kei Saito ◽

Haru-aki Yanagisawa ◽

Toshiki Yagi ◽

Ritsu Kamiya ◽

...

Keyword(s):

Light Chain ◽

Regulatory Mechanism ◽

Binding Domain ◽

Particle Analysis ◽

Dynein Light Chain ◽

Microtubule Binding ◽

Heavy Chains ◽

Microtubule Binding Domain ◽

Axonemal Dynein ◽

Force Generator

The outer arm dynein (OAD) complex is the main propulsive force generator for ciliary/flagellar beating. In Chlamydomonas and Tetrahymena, the OAD complex comprises three heavy chains (α, β, and γ HCs) and >10 smaller subunits. Dynein light chain-1 (LC1) is an essential component of OAD. It is known to associate with the Chlamydomonas γ head domain, but its precise localization within the γ head and regulatory mechanism of the OAD complex remain unclear. Here Ni-NTA-nanogold labeling electron microscopy localized LC1 to the stalk tip of the γ head. Single-particle analysis detected an additional structure, most likely corresponding to LC1, near the microtubule-binding domain (MTBD), located at the stalk tip. Pull-down assays confirmed that LC1 bound specifically to the γ MTBD region. Together with observations that LC1 decreased the affinity of the γ MTBD for microtubules, we present a new model in which LC1 regulates OAD activity by modulating γ MTBD's affinity for the doublet microtubule.

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