Temporal and spatial localization of type I and II collagens in human thyroid cartilage

Precise knowledge of the level of the vocal fold as projected on the external thyroid cartilage is of critical importance for the performance of thyroplasty type I and supraglottic laryngectomy. Measurements of the external laryngeal framework were made on the larynges of 18 human cadavers in order to identify landmarks that will aid the surgeon in determining endolaryngeal anatomy. On the basis of our results, the following guidelines are recommended: (1) Thyroid cartilage incision for supra-glottic laryngectomy should be made on a line joining the juncture of the upper one third and lower two thirds of the midline length and the juncture of the upper one third and lower two thirds of the oblique line. This will ensure a position above the level of the anterior commissure and the true vocal cord; (2) In thyroplasty type I, the superior border of the thyroid cartilage window should be made at a line joining the midpoint of the midline length and the juncture of the upper two thirds and lower one third of the oblique line. Formation of the cartilage window according to this guideline will ensure its placement lateral to the vocalis muscle.

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Expression of insulin-like growth factor receptors in primary human thyroid neoplasms

Acta Endocrinologica ◽

10.1530/acta.0.1210112 ◽

1989 ◽

Vol 121 (1) ◽

pp. 112-120 ◽

Cited By ~ 38

Author(s):

Tohru Yashiro ◽

Yoshito Ohba ◽

Hitomi Murakami ◽

Takao Obara ◽

Toshio Tsushima ◽

...

Keyword(s):

Thyroid Cancer ◽

Binding Capacity ◽

Specific Binding ◽

Human Thyroid ◽

Scatchard Analysis ◽

Type I ◽

Single Class ◽

Normal Tissues ◽

Igf I ◽

Cancer Tissues

Abstract. The presence of IGF-I receptors was demonstrated in normal and neoplastic tissues of human thyroid. Binding of [125I]IGF-I to thyroid membranes was dependent on time and temperature of incubation, and maximal binding was achieved at 4°C and 18 h of incubation. [125I] IGF-I binding was dose-dependently displaced by unlabelled IGF-I; half-maximal inhibition occurred at concentrations of 10–20 μg/l. IGF-II and insulin had relative potencies of 5 and 1% compared with IGF-I. Scatchard analysis of binding data revealed a single class of IGF-I receptors with high affinity (Ka: 1.2–8.6 × 109 1/mol) in normal thyroid tissues. Affinity cross-linking and autoradiography demonstrated the type I IGF receptors. Specific binding of [125I] IGF-I in thyroid cancer tissues (9.69 ± 2.07% per 200 μg protein; mean ± sem, N = 8) was significantly (p <0.05) higher than that in the surrounding normal tissues (3.03 ± 0.35%, N = 8). In contrast, there was no difference in the binding between adenoma tissues (4.19 ± 0.53%, N = 5) and the adjacent normal tissues (2.94 ± 0.24%, N = 5). The higher IGF-I binding in cancer tissues was due to an increase in the binding capacity without any change in the affinity. The presence of IGF-I receptors suggests a possible role of IGF-I and its receptors in the growth of thyroid cancer cells.

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Elastin exhibits a distinctive temporal and spatial pattern of distribution in the developing chick limb in association with the establishment of the cartilaginous skeleton

Journal of Cell Science ◽

10.1242/jcs.107.9.2623 ◽

1994 ◽

Vol 107 (9) ◽

pp. 2623-2634 ◽

Cited By ~ 1

Author(s):

J.M. Hurle ◽

G. Corson ◽

K. Daniels ◽

R.S. Reiter ◽

L.Y. Sakai ◽

...

Keyword(s):

Extracellular Matrix ◽

Spatial Pattern ◽

Elastic Fiber ◽

Spatial Location ◽

Limb Bud ◽

Confocal Laser ◽

Elastic Fibers ◽

Type I ◽

Temporal And Spatial

In this work we have analyzed the presence of elastic components in the extracellular matrices of the developing chick leg bud. The distributions of elastin and fibrillin were studied immunohistochemically in whole-mount preparations using confocal laser microscopy. The association of these constituents of the elastic matrix with other components of the extracellular matrix was also studied, using several additional antibodies. Our results reveal the transient presence of an elastin-rich scaffold of extracellular matrix fibrillar material in association with the establishment of the cartilaginous skeleton of the leg bud. The scaffold consisted of elastin-positive fibers extending from the ectodermal surface of the limb to the central cartilage-forming regions and between adjacent cartilages. Fibrillin immunolabeling was negative in this fibrillar scaffold while other components of the extracellular matrix including: tenascin, laminin and collagens type I, type III and type VI; appeared codistributed with elastin in some regions of the scaffold. Progressive changes in the spatial pattern of distribution of the elastin-positive scaffold were detected in explant cultures in which one expects a modification in the mechanical stresses of the tissues related to growth. A scaffold of elastin comparable to that found in vivo was also observed in high-density micromass cultures of isolated limb mesodermal cells. In this case the elastic fibers are observed filling the spaces located between the cartilaginous nodules. The fibers become reoriented and attach to the ectodermal basal surface when an ectodermal fragment is located at the top of the growing micromass. Our results suggest that the formation of the cartilaginous skeleton of the limb involves the segregation of the undifferentiated limb mesenchyme into chondrogenic and elastogenic cell lineages. Further, a role for the elastic fiber scaffold in coordinating the size and the spatial location of the cartilaginous skeletal elements within the limb bud is also suggested from our observations.

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Detection of SARS-COV-2 receptor ACE-2 mRNA in thyroid cells: a clue for COVID-19-related subacute thyroiditis

Journal of Endocrinological Investigation ◽

10.1007/s40618-020-01436-w ◽

2020 ◽

Author(s):

M. Rotondi ◽

F. Coperchini ◽

G. Ricci ◽

M. Denegri ◽

L. Croce ◽

...

Keyword(s):

Primary Cultures ◽

Thyroid Tissue ◽

Subacute Thyroiditis ◽

Human Thyroid ◽

Thyroid Cell ◽

Type I ◽

Rt Pcr ◽

Follicular Cells ◽

Thyroid Cells ◽

Tissue Samples

Abstract Purpose SARS-COV-2 is a pathogenic agent belonging to the coronavirus family, responsible for the current global world pandemic. Angiotensin-converting enzyme 2 (ACE-2) is the receptor for cellular entry of SARS-CoV-2. ACE-2 is a type I transmembrane metallo-carboxypeptidase involved in the Renin-Angiotensin pathway. By analyzing two independent databases, ACE-2 was identified in several human tissues including the thyroid. Although some cases of COVID-19-related subacute thyroiditis were recently described, direct proof for the expression of the ACE-2 mRNA in thyroid cells is still lacking. Aim of the present study was to investigate by RT-PCR whether the mRNA encoding for ACE-2 is present in human thyroid cells. Methods RT-PCR was performed on in vitro ex vivo study on thyroid tissue samples (15 patients undergoing thyroidectomy for benign thyroid nodules) and primary thyroid cell cultures. Results The ACE-2 mRNA was detected in all surgical thyroid tissue samples (n = 15). Compared with two reporter genes (GAPDH: 0.052 ± 0.0026 Cycles−1; β-actin: 0.044 ± 0.0025 Cycles−1; ACE-2: 0.035 ± 0.0024 Cycles−1), the mean level of transcript expression for ACE-2 mRNA was abundant. The expression of ACE-2 mRNA in follicular cells was confirmed by analyzing primary cultures of thyroid cells, which expressed the ACE-2 mRNA at levels similar to tissues. Conclusions The results of the present study demonstrate that the mRNA encoding for the ACE-2 receptor is expressed in thyroid follicular cells, making them a potential target for SARS-COV-2 entry. Future clinical studies in patients with COVID-19 will be required for increase our understanding of the thyroid repercussions of SARS-CoV-2 infection.

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Temporal and spatial localization of prothymosin ? transcript in the Harderian gland of the frog,Rana esculenta

Journal of Experimental Zoology ◽

10.1002/jez.10097 ◽

2002 ◽

Vol 292 (7) ◽

pp. 633-639 ◽

Cited By ~ 9

Author(s):

Gianluca de Rienzo ◽

Rona di Sena ◽

Diana Ferrara ◽

Carmela Palmiero ◽

Gabriella Chieffi Baccari ◽

...

Keyword(s):

Spatial Localization ◽

Harderian Gland ◽

Rana Esculenta ◽

Temporal And Spatial

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Temporal and Spatial Localization of Novel Nuclear Protein NP95 in Mitotic and Meiotic Cells.

Cell Structure and Function ◽

10.1247/csf.25.149 ◽

2000 ◽

Vol 25 (3) ◽

pp. 149-159 ◽

Cited By ~ 43

Author(s):

Takatoshi Uemura ◽

Eiko Kubo ◽

Yasuyoshi Kanari ◽

Toshimiti Ikemura ◽

Kouichi Tatsumi ◽

...

Keyword(s):

Nuclear Protein ◽

Spatial Localization ◽

Temporal And Spatial

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In vitro morphogenesis of chick embryo hypertrophic cartilage.

The Journal of Cell Biology ◽

10.1083/jcb.105.2.999 ◽

1987 ◽

Vol 105 (2) ◽

pp. 999-1006 ◽

Cited By ~ 49

Author(s):

C Tacchetti ◽

R Quarto ◽

L Nitsch ◽

D J Hartmann ◽

R Cancedda

Keyword(s):

Chick Embryo ◽

Type I ◽

Cell Aggregates ◽

In Vitro Morphogenesis ◽

Temporal And Spatial Distribution ◽

Hypertrophic Cartilage ◽

Histologic Appearance ◽

Temporal And Spatial

Dedifferentiated chick embryo chondrocytes (Castagnola, P., G. Moro, F. Descalzi-Cancedda, and R. Cancedda, 1986, J. Cell Biol., 102:2310-2317), when transferred to suspension culture on agarose-coated dishes in the presence of ascorbic acid, aggregate and remain clustered. With time in culture, clusters grow in size and adhere to each other, forming structures that may be several millimeters in dimension. These structures after 7 d of culture have the histologic appearance of mature hypertrophic cartilage partially surrounded by a layer of elongated cells resembling the perichondrium. Cells inside the aggregates have ultrastructural features of stage I (proliferating) or stage II (hypertrophic) chondrocytes depending on their location. Occurrence and distribution of type I, II, and X collagens in the in vitro-formed cartilage at different times of culture, show a temporal and spatial distribution of these antigens reminiscent of the maturation events occurring in the cartilage in vivo. A comparable histologic appearance is shown also by cell aggregates obtained starting with a population of cells derived from a single, cloned, dedifferentiated chondrocyte.

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